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Protein Kinesis: Getting

Proteins to Their Destination
Proteins are the major building blocks of life. Eukaryotic cells
synthesize proteins for thousands of different functions. Some
examples:

• to build the components of the cytosol (e.g. microtubules, glycolytic

enzymes);
• to build the receptors and other molecules exposed at the surface of the cell
embedded in the plasma membrane;
• to supply some of the components of the mitochondria and (in plant cells)
chloroplasts;
• proteins secreted from the cell to supply the needs
of other cells and tissues (e.g. collagen to support
cells, hormones to signal them).

All proteins are synthesized by ribosomes using

the information encoded in molecules of
messenger RNA (mRNA). This process is called
translation and is described in Gene Translation:
RNA -> Protein. Our task here is to explore the
ways that these proteins are delivered to their
proper destinations.
The various destinations for proteins occur in two major
sets:

• one set for those proteins synthesized by

ribosomes that remain suspended in the cytosol,
and
• a second set for proteins synthesized by ribosomes
that are attached to the membranes of the
endoplasmic reticulum (ER) forming "rough endoplasmic reticulum" (RER).
This electron micrograph (courtesy of Keith Porter) shows the RER in a bat
pancreas cell. The clearer areas are the lumens.

So the first decision that must be made as a ribosome begins to translate a mRNA
into a polypeptide is whether to remain free in the cytosol or to bind to the ER.

Pathways Through the Endoplasmic

Reticulum (ER)
 The decision to enter the ER is dictated by the presence of
a signal sequence on the growing polypeptide.

The Signal Sequence

The signal sequence consists of the first portion

of the elongating polypeptide chain (so the
signal sequence occurs at the amino terminal of
the polypeptide). Typical signal sequences
contain 15 - 30 amino acids. The precise amino
acid sequence varies surprisingly from one
protein to the next, but all signal sequences
include many hydrophobic amino acids.
The 1999 Nobel Prize in Physiology or Medicine was awarded on October 11, 1999 to
Dr. Günter Blobel for his discovery of the signal sequence and other intrinsic signals
that enable proteins to reach their proper destinations.
If a signal sequence is present,

• translation ceases after it has been synthesized

• the signal sequence is recognized by and is bound by a signal recognition
particle (SRP)
• the complex of ribosome with its nascent polypeptide and the SRP binds to a
receptor on the surface (facing the cytosol) of the ER.
• the SRP leaves and translation recommences
• the growing polypeptide chain is extruded through a pore in the ER
membrane and into the lumen of the ER.
• the signal sequence is usually clipped off the polypeptide unless the
polypeptide is to be retained as an integral membrane protein.
• other proteins, called molecular chaperones, present in the lumen of the
ER, bind the growing polypeptide chain and assist it to fold into its correct
tertiary structure.
• sugar residues may be added to the protein. The process is called
glycosylation and often is essential for proper folding of the final product, a
glycoprotein.

Destinations of proteins synthesized within the ER

Proteins synthesized within the ER are transported to the Golgi apparatus. Portions
of the ER are pinched off, forming transport vesicles. These carry their load of
proteins to the Golgi apparatus. The membrane of the transport vesicle fuses with
the membrane of the Golgi apparatus, merging their contents. Further steps of
glycosylation may occur within the Golgi apparatus. The exact pattern of
glycosylation determines the final destination of the proteins. There are two options.

• proteins glycosylated with residues of mannose-6-phosphate will leave the

Golgi in transport vesicles that eventually fuse with lysosomes (path 2 in the
figure).
 • proteins that do not receive this marker, leave in transport vesicles that
eventually fuse with the plasma membrane (path 1 in the figure). These
are:
o integral membrane proteins that become exposed at the surface of the
cell (forming receptors and the like) and
o proteins in solution within the transport vesicle. These are discharged
from the cell. This secretory process is called exocytosis.

The Signal Recognition Particle (SRP)

The signal recognition particle in mammalian cells is made from:

• a single small (7S) molecule of RNA

• six different molecules of protein

It contains binding sites for:

• the signal sequence

• the ribosome, and
• an SRP receptor, also called the docking protein, on the cytosol face of the
membranes of the ER.

[Return to signal sequence]

Destinations of Proteins Synthesized By

Free Ribosomes
Ribosomes synthesizing a protein without a signal sequence do not bind to the ER
and continue synthesis until the polypeptide is completed. Chaperones are also
present in the cytosol that help the protein assume its final three-dimensional
configuration. Some of the important destinations for these proteins are:

• The cytosol itself. Such proteins as

o the enzymes of glycolysis
o tubulins for making microtubules
o actin for making microfilaments

are simply released from the ribosome and go to work.

• The nucleus. Many proteins - histones, transcription factors, and

ribosomal proteins are notable examples - must move from the cytosol into
the interior of the nucleus. They are targeted to the nucleus by their nuclear
localization sequence, a sequence of 7 - 41 amino acids of which the basic
amino acids lysine and arginine are characteristic members. These proteins
are actively transported through pores in the nuclear envelope into the
interior.
• Mitochondria. Although the mitochondrion has its own genome [View] and
protein synthesizing machinery, most of the proteins used by mitochondria
are
 o encoded by genes in the nucleus of the cell
o synthesized in the cytosol,
o must be imported into the mitochondrion.

Proteins destined for mitochondrion contain a characteristic signal sequence.

This is recognized and bound by a chaperone called mitochondrial
stimulation factor (MSF). MSF targets the protein to a receptor embedded
in the outer membrane of the mitochondrion. Other factors and receptors
shepherd proteins through the intermembrane space to the inner
mitochondrial membrane (e.g. some proteins of the respiratory chain) and
the matrix.

• Chloroplasts. Chloroplasts, like mitochondria, have their own genome [View]

and their own protein-synthesizing machinery. But also like mitochondria,
most of the proteins used in chloroplasts are encoded by genes in the nucleus
of the cell, are synthesized by ribosomes in the cytosol, and must then be
imported into the chloroplast. Proteins destined for chloroplasts are
recognized by their characteristic transit sequence. Chaperones are also
needed to get them to their final destination: stroma, thylakoid membrane,
etc.
• Peroxisomes. Proteins destined for peroxisomes are synthesized with a
peroxisomal targeting signal (PTS) that binds to a receptor molecule that
takes the protein into the peroxisome and then returns for another load.

Two peroxisomal targeting signals have been identified:

o a 9-amino acid sequence at the N-terminal of the protein;

o a tripeptide at the C-terminal.

Each has its own receptor to take it to the peroxisome.

Gene Translation: RNA ->

Protein
 Index to this page
• The RNA Codons
• Steps
o 1. Initiation
o 2. Elongation
The problem: o 3. Termination
How does a • Polysomes
particular • Quality Control
o Nonsense-Mediated mRNA Decay
sequence of
o Nonstop mRNA Decay
nucleotides • Regulation of Translation
specify a o RNA Interference
particular o Some Riboswitches
sequence of
amino • Summary
acids?
The answer: by means of transfer RNA molecules,
each specific for one amino acid and for a particular
triplet of nucleotides in mRNA called a codon. The
family of tRNA molecules enables the codons in a mRNA molecule to
be translated into the sequence of amino acids in the protein.

This image shows the structure of alanine transfer RNA (tRNAala)

from yeast. It consists of a single strand of 77 ribonucleotides. The
chain is folded on itself, and many of the bases pair with each other
forming four helical regions. Loops are formed in the unpaired regions
of the chain. (The bases circled in blue have been chemically-modified
following synthesis of the molecule.)
At least one kind of tRNA is present for each of the 20 amino acids
used in protein synthesis. (Some amino acids employ the services of
two or three different tRNAs, so most cells contain as many as 32
different kinds of tRNA.) The amino acid is attached to the appropriate
tRNA by an activating enzyme (one of 20 aminoacyl-tRNA
synthetases) specific for that amino acid as well as for the tRNA
assigned to it.
Each kind of tRNA has a sequence of 3 unpaired nucleotides - the anticodon - which
can bind, following the rules of base pairing, to the complementary triplet of
nucleotides - the codon - in a messenger RNA (mRNA) molecule. Just as DNA
replication and transcription involve base pairing of nucleotides running in opposite
direction, so the reading of codons in mRNA (5' -> 3') requires that the anticodons
bind in the opposite direction.
Anticodon: 3' CGA 5'
Codon: 5' GCU 3'

The RNA Codons

Second nucleotide
U C A G
 UUU Phenylalanine UCU Serine UAU Tyrosine UGU Cysteine
U
(Phe) (Ser) (Tyr) (Cys)
UUC Phe UCC Ser UAC Tyr UGC Cys C
U
UUA Leucine (Leu) UCA Ser UAA STOP UGA STOP A
UGG Tryptophan
UUG Leu UCG Ser UAG STOP G
(Trp)
CCU Proline CAU Histidine CGU Arginine
CUU Leucine (Leu) U
(Pro) (His) (Arg)
CUC Leu CCC Pro CAC His CGC Arg C
C
CAA Glutamine
CUA Leu CCA Pro CGA Arg A
(Gln)
CUG Leu CCG Pro CAG Gln CGG Arg G
ACU Threonine AAU Asparagine
AUU Isoleucine (Ile) AGU Serine (Ser) U
(Thr) (Asn)
AUC Ile ACC Thr AAC Asn AGC Ser C
A AGA Arginine
AUA Ile ACA Thr AAA Lysine (Lys) A
(Arg)
AUG Methionine (Met)
ACG Thr AAG Lys AGG Arg G
or START
GCU Alanine GAU Aspartic acid GGU Glycine
GUU Valine Val U
(Ala) (Asp) (Gly)
GUC (Val) GCC Ala GAC Asp GGC Gly C
G
GAA Glutamic
GUA Val GCA Ala GGA Gly A
acid (Glu)
GUG Val GCG Ala GAG Glu GGG Gly G
Note:

• Most of the amino acids are encoded by synonymous codons that differ in the
third position of the codon.
• In some cases, a single tRNA can recognize two or more of these synonymous
codons.
• Example: phenylalanine tRNA with the anticodon 3' AAG 5' recognizes not
only UUC but also UUU.
• The violation of the usual rules of base pairing at the third nucleotide of a
codon is called "wobble"
• The codon AUG serves two related functions
o It begins every message; that is, it signals the start of translation
placing the amino acid methionine at the amino terminal of the
polypeptide to be synthesized.
o When it occurs within a message, it guides the incorporation of
methionine.
• Three codons, UAA, UAG, and UGA, act as signals to terminate translation.
They are called STOP codons.

The Steps of Translation

 1. Initiation

• The small subunit of the ribosome binds to a

site "upstream" (on the 5' side) of the start of
the message.
• It proceeds downstream (5' -> 3') until it
encounters the start codon AUG.
• Here it is joined by the large subunit and a
special initiator tRNA.
• The initiator tRNA binds to the P site (shown
in pink) on the ribosome.
• In eukaryotes, initiator tRNA carries
methionine (Met). (Bacteria use a modified
methionine designated fMet.)

2. Elongation

• An aminoacyl-tRNA (a tRNA covalently

bound to its amino acid) able to base pair with
the next codon on the mRNA arrives at the A
site (green) associated with:
o an elongation factor (called EF-Tu in
bacteria)
o GTP (the source of the needed energy)
• The preceding amino acid (Met at the start of translation) is covalently linked
to the incoming amino acid with a peptide bond (shown in red).
• The initiator tRNA is released from the P site.
• The ribosome moves one codon downstream.
• This shifts the more recently-arrived tRNA, with its attached peptide, to the P
site and opens the A site for the arrival of a new aminoacyl-tRNA.
• This last step is promoted by another protein elongation factor (named EF-
G) and the energy of another molecule of GTP.

Note: the initiator tRNA is the only member of the tRNA family that can
bind directly to the P site. The P site is so-named because, with the
exception of initiator tRNA, it binds only to a peptidyl-tRNA molecule;
that is, a tRNA with the growing peptide attached.
The A site is so-named because it binds only to the incoming
aminoacyl-tRNA; that is the tRNA bringing the next amino acid. So, for
example, the tRNA that brings Met into the interior of the polypeptide
can bind only to the A site.

3. Termination

• The end of the message is marked by one or more STOP codons (UAA, UAG,
UGA).
• There are no tRNA molecules with anticodons for STOP codons.
(With a few special exceptions: link to mitochondrial genes and to nonstandard
amino acids.)
 • However, a protein release factor recognizes these codons when they arrive
at the A site.
• Binding of this protein releases the polypeptide from the ribosome.
• The ribosome splits into its subunits, which can later be reassembled for
another round of protein synthesis.

Polysomes
A single mRNA molecule usually has many ribosomes traveling along it, in various
stages of synthesizing the polypeptide. This complex is called a polysome [View].

Quality Control
Mutations or faulty transcription can produce mRNA molecules that have

• premature STOP codons. Translation of these produces a truncated protein

that is probably ineffective and may be harmful. The problem is solved by
Nonsense-Mediated mRNA Decay (NMD).
• no STOP codon. These produce "nonstop" transcripts. The problem is solved
by Nonstop mRNA Decay.

Nonsense-Mediated mRNA Decay (NMD)

Premature stop codons (PTCs) may be generated by

• mutations, especially frameshifts;

• RNA processing (intron removal) errors;
• as an inevitable consequence of creating antigen receptors on B cells and T
cells. [Link to discussion.]

Mechanism

• During RNA processing within the nucleus, protein complexes are added at
each spot where adjacent exons are spliced together. (These are important
signals for exporting the mRNA to the cytoplasm.)
• In the cytoplasm, as the ribosome moves down the mRNA, these complexes
are removed (and sent back to the nucleus for reuse).
• If the ribosome encounters a premature STOP codon, the final exon-exon
tag(s) are not removed, and this marks the defective mRNA for destruction.

Nonstop mRNA Decay

Nonstop transcripts occur when there is no STOP codon in the

message. As a result the ribosome is unable to recruit the release
factors needed to leave the mRNA.
Nonstop transcripts are formed during RNA processing, e.g., by having the poly(A)
tail put on before the STOP codon is reached.
Mechanisms

Eukaryotes and prokaryotes handle the problem of no STOP codon

differently.

• In eukaryotes, when the ribosome stalls at the end of the poly(A) tail,
proteins are recruited to
o release the ribosome for reuse and to
o degrade the faulty message.
• In prokaryotes, a special RNA molecule - called tmRNA saves the day. It is
called tmRNA because it has the properties of both a transfer RNA and a
messenger RNA.
o The transfer part adds alanine to the A site on the ribosome.
o The ribosome then moves on to the messenger part which encodes 10
amino acids that target the molecule for destruction (and releases the
ribosome for reuse).

Regulation of Translation
The expression of most genes is controlled at the level of their
transcription. Transcription factors (proteins) bind to promoters and
enhancers turning on (or off) the genes they control.
Link to an example.
However, there are some cases where gene expression is controlled at
the level of translation instead.

RNA Interference

Here small RNA molecules bind to the complementary portion of a mRNA and

• prevent it from being translated by ribosomes or

• trigger its destruction.

Link to a discussion.

Some Riboswitches

In many bacteria (and some eukaryotes), it turns out that the

regulation of the level of certain metabolites is controlled by
riboswitches. A riboswitch is a molecule of messenger RNA (mRNA)
which has a specific binding site for the metabolite (or a close relative).
Examples:

• If thiamine pyrophosphate (the active form of thiamine [vitamin B1]) is

available in the culture medium of E. coli,
 o it binds to a messenger RNA whose protein product is an enzyme
needed to synthesize thiamine from the ingredients in minimal
medium.
o Binding induces an allosteric shift in the structure of the mRNA so that
it can no longer bind to a ribosome and thus cannot be translated into
the enzyme.
o E. coli no longer wastes resources on synthesizing a vitamin that is
available preformed.
• If vitamin B12 is present in the cell,
o it binds to the mRNA which encodes a protein needed to import the
vitamin from the culture medium.
o This, too, induces an allosteric shift in the mRNA that prevents it from
binding a ribosome.
o E. coli no longer wastes resources on synthesizing a transporter for a
vitamin that it already has enough of.

Other riboswitches act on transcription rather than translation. [Link]

It has been suggested that these regulatory mechanisms, which do not
involve any protein, are a relict from an "RNA world".

Summary
Gene expression occurs in two steps:

• transcription of the information encoded in DNA into a molecule of RNA

(discussed in Gene Expression: Transcription) and
• translation of the information encoded in the nucleotides of mRNA into a
defined sequence of amino acids in a protein (discussed here).

In eukaryotes, the processes of transcription and translation are

separated both spatially and in time. Transcription of DNA into mRNA
occurs in the nucleus. Translation of mRNA into polypeptides occurs on
polysomes in the cytoplasm.
In prokaryotes (which have no nucleus), both these steps of gene
expression occur simultaneously: the nascent mRNA molecule begins
to be translated even before its transcription from DNA is complete.
View an electron micrograph showing polysomes formed during simultaneous
transcription and translation in E. coli.
Recent evidence (reported by Iborra, et. al, in the 10 August 2001 issue of Science)
shows that the distinction between prokaryotes and eukaryotes is not absolute. They
find that 10 to 15% of translation in mammalian cells occurs in the nucleus, and that
at least some of this translation occurs as the mRNA is still being synthesized by RNA
polymerase (just as in E. coli)

Cellular Respiration
 Index to this page
• Mitochondria
Cellular respiration is the process of • The Citric Acid Cycle
oxidizing food molecules, like glucose, • The Respiratory Chain
to carbon dioxide and water. The • Chemiosmosis in Mitochondria
energy released is trapped in the form • How many ATPs?
of ATP for use by all the energy-
consuming activities of the cell. • Mitochondrial DNA (mtDNA)
The process occurs in two phases:

• glycolysis, the breakdown of glucose to pyruvic acid

• the complete oxidation of pyruvic acid to carbon dioxide and
water

In eukaryotes, glycolysis occurs in the cytosol. (Link to a discussion of

glycolysis). The remaining processes take place in mitochondria.

Mitochondria
Mitochondria are membrane-enclosed organelles distributed through the cytosol of
most eukaryotic cells. Their main function is the conversion of the potential energy of
food molecules into ATP. Mitochondria have:

• an outer membrane that encloses the entire structure

• an inner membrane that encloses a fluid-filled matrix
• between the two is the intermembrane space
• the inner membrane is elaborately folded with shelflike cristae projecting into
the matrix.
• a small number (some 5-10) circular molecules of DNA

The Outer Membrane

The outer membrane contains many complexes of integral membrane proteins that
form channels through which a variety of molecules and ions move in and out of the
mitochondrion.

The Inner Membrane

The inner membrane contains 5 complexes of integral membrane proteins:

• NADH dehydrogenase
• succinate dehydrogenase
• cytochrome c reductase(also known as the cytochrome b-c1 complex)
• cytochrome c oxidase
• ATP synthase

The Matrix
 The matrix contains a complex
mixture of soluble enzymes that
catalyze the respiration of pyruvic
acid and other small organic
molecules.
Here pyruvic acid is

• oxidized by NAD+ producing NADH

+ H+
• decarboxylated producing a
molecule of
o carbon dioxide (CO2) and
o a 2-carbon fragment of
acetate bound to coenzyme
A forming acetyl-CoA

The Citric Acid Cycle

• This 2-carbon fragment is donated to a molecule of
oxaloacetic acid.
• The resulting molecule of citric acid (which gives its name to
the process) undergoes the series of enzymatic steps shown
in the diagram.
• The final step regenerates a molecule of oxaloacetic acid and the cycle is
ready to turn again.

Summary:

• Each of the 3 carbon atoms present in the pyruvate that entered the
mitochondrion leaves as a molecule of carbon dioxide (CO2).
• At 4 steps, a pair of electrons (2e-) is removed and transferred to NAD+
reducing it to NADH + H+.
• At one step, a pair of electrons is removed from succinic acid and reduces
FAD to FADH2.

The electrons of NADH and FADH2 are transferred to the respiratory

chain.

The Respiratory Chain

The respiratory chain consists of 3 complexes of integral membrane proteins

• the NADH dehydrogenase complex

• the cytochrome c reductase complex
• the cytochrome c oxidase complex

and two freely-diffusible molecules

 • ubiquinone
• cytochrome c

that shuttle electrons from one complex to the next.

The respiratory chain accomplishes:

• the stepwise transfer of electrons from NADH (and FADH2) to oxygen

molecules to form (with the aid of protons) water molecules (H2O);

(Cytochrome c can only transfer one electron at a time, so

cytochrome c oxidase must wait until it has accumulated 4 of
them before it can react with oxygen.)

• harnessing the energy released by this transfer to the pumping of protons

(H+) from the matrix to the intermembrane space.
• Approximately 20 protons are pumped into the intermembrane space as the 4
electrons needed to reduce oxygen to water pass through the respiratory
chain.
• The gradient of protons formed across the inner membrane by this process of
active transport forms a miniature battery.
• The protons can flow back down this gradient, reentering the matrix, only
through another complex of integral proteins in the inner membrane, the ATP
synthase complex (as we shall now see).

Chemiosmosis in mitochondria
The energy released as electrons pass down the gradient from NADH
to oxygen is harnessed by the three enzyme complexes of the
respiratory chain to pump protons (H+) against their concentration
gradient from the matrix of the mitochondrion into the
intermembrane space (an example of active transport).

As their concentration increases there (which is the same as saying

that the pH decreases), a strong diffusion gradient is set up. The only
exit for these protons is through the ATP synthase complex. As in
chloroplasts, the energy released as these electrons flow down their
gradient is harnessed to the synthesis of ATP. The process is called
chemiosmosis and is an example of facilitated diffusion.
One-half of the 1997 Nobel Prize in Chemistry was awarded to Paul D.
Boyer and John E. Walker for their discovery of how ATP synthase
works.

How many ATPs?

It is tempting to try to view the synthesis of ATP as a simple matter of
stoichiometry (the fixed ratios of reactants to products in a chemical
reaction). But (with 3 exceptions) it is not.
Most of the ATP is generated by the proton gradient that develops
across the inner mitochondrial membrane. The number of protons
pumped out as electrons drop from NADH through the respiratory
chain to oxygen is theoretically large enough to generate, as they
return through ATP synthase, 3 ATPs per electron pair (but only 2 ATPs
for each pair donated by FADH2).
With 12 pairs of electrons removed from each glucose molecule,

• 10 by NAD+ (so 10x3=30); and

• 2 by FADH2 (so 2x2=4),

this could generate 34 ATPs.

Add to this the 4 ATPs that are generated by the 3 exceptions and one
arrives at 38.
But

• The energy stored in the proton gradient is used for a number of other
mitochondrial functions such as the active transport of a variety of essential
molecules and ions through the mitochondrial membranes.
• NADH is also used as reducing agent for many cellular reactions.

So the actual yield of ATP as mitochondria respire varies with

conditions. It probably seldom exceeds 30.

The three exceptions

A stoichiometric production of ATP does occur at:

• one step in the citric acid cycle yielding 2 ATPs for each glucose molecule.
This step is the conversion of alpha-ketoglutaric acid to succinic acid.
• at two steps in glycolysis yielding 2 ATPs for each glucose molecule.

Mitochondrial DNA (mtDNA)

 The human mitochondrion contains 5-10 identical,
circular molecules of DNA. Each consists of 16,569
base pairs carrying the information for 37 genes
which encode:

• 2 different molecules of ribosomal RNA (rRNA)

• 22 different molecules of transfer RNA (tRNA) (at
least one for each amino acid)
• 13 polypeptides

The rRNA and tRNA molecules are used in the

machinery that synthesizes the 13 polypeptides.
The 13 polypeptides are subunits of the protein complexes in the inner
mitochondrial membrane, including subunits of NADH
dehydrogenase, cytochrome c oxidase, and ATP synthase.
However, each of these protein complexes also requires subunits that
are encoded by nuclear genes, synthesized in the cytosol, and
imported from the cytosol into the mitochondrion.

Mutations in mtDNA cause human diseases.

A number of human diseases are caused by mutations in genes in our mitochondria:

• cytochrome b
• 12S rRNA
• ATP synthase
• subunits of NADH dehydrogenase
• several tRNA genes

Although many different organs may be affected, disorders of the brain

and muscles are the most common. Perhaps this reflects the great
demand for energy of both these organs.
Some of these disorders are inherited in the germline. In every case,
the mutant gene is received from the mother because none of the
mitochondria in sperm survives in the fertilized egg. Other disorders
are somatic; that is, the mutation occurs in the somatic tissues of the
individual.

Example: exercise intolerance

A number of humans who suffer from easily-fatigued muscles turn out to have a
mutations in their cytochrome b gene. Curiously, only the mitochondria in their
muscles have the mutation; the mtDNA of their other tissues is normal. Presumably,
very early in their embryonic development, a mutation occurred in the cytochrome b
gene in a cell destined to produce their muscles.

Why do mitochondria have their own genome?

Many of the features of the mitochondrial genetic system resemble
those found in prokaryotes like bacteria. This has strengthened the
theory that mitochondria are the evolutionary descendants of a
prokaryote that established an endosymbiotic relationship with the
ancestors of eukaryotic cells early in the history of life on earth.
However, many of the genes needed for mitochondrial function have
since moved to the nuclear genome.
The recent sequencing of the complete genome of Rickettsia
prowazekii has revealed a number of genes closely related to those
found in mitochondria. Perhaps rickettsias are the closest living
descendants of the endosymbionts that became the mitochondria of
eukaryotes.