Theme 2C Flashcards

1
Q

What are the three components of translational regulation of gene expression?

A
  1. Initiation
  2. Elongation
  3. Termination
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2
Q

What is translation?

A

The assembly of amino acids into polypeptides/proteins

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3
Q

What do amino acids contain?

A
  • Amino group
  • Carboxyl group
  • R group (variable and determines unique character of amino acid)
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4
Q

What is a dehydration reaction?

A

Two amino acids are joined together via a covalent peptide bond between the carboxyl group and amino group

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5
Q

What are polypeptides?

A

Linear chains of amino acids linked by peptide bonds

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6
Q

What are proteins?

A

Folded (3D structure) and contain multiple polypeptides

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7
Q

What are non-polar amino acids?

A

R groups are usually CH2 or CH3, and not soluble in water

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8
Q

What are uncharged polar amino acids?

A

R groups usually contain oxygen (hydroxyl group or double bond)

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9
Q

What are charged amino acids?

A

R groups contain acids or bases that can ionize (have a positive or negative charge)

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10
Q

What are aromatic amino acids?

A

R groups that contain a carbon ring with alternating single and double bonds

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11
Q

What are the special functional amino acids?

A
  1. Methionine: first amino acid in polypeptide (start codon)
  2. Proline: causes bend in polypeptide chains
  3. Cysteine: disulfide bridge (2 cysteins next to each other) contributes to structure of polypeptides
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12
Q

What is the primary protein structure?

A

Amino acid sequence, determines protein folding and 3D structure which is critical for proper function

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13
Q

What is the secondary protein structure?

A

has alpha helices and beta sheets, depends on hydrogen bonding in the polypeptide backbone

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14
Q

What is the tertiary protein structure?

A

The 3D structure of a single polypeptide and is composed of interactions between amino acid side chains (disulfide bonds and charged regions)

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15
Q

What is the quaternary protein structure?

A

Interactions between more than one polypeptide to form a multisubunit protein (like hemoglobin)

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16
Q

What are chaperones?

A

Function to protect slow-folding or denatured proteins by preventing their aggregation

17
Q

What are codons?

A

They are written in the 5’-3’ as they appear in mRNA.
- UAG, UAA, and UGA are stop codons and do not code for amino acids
- Non-overlapping, message contains no gaps
- Message translated in fixed reading frame set by start codon

18
Q

What is degeneracy in the genetic code?

A

Most amino acids are specified by more than one codon

19
Q

What are tRNA’s?

A

The adaptor between codons (mRNA0 and amino acids.
- Acceptor stem is where amino acid is attached
- Anticodon is at the bottom loop of the tRNA contains a 3 nucleotide sequence that recognizes the mRNA codon
- tRNA molecules do not bind to stop codons

20
Q

What is wobble pairing?

A

The base at the 5’ end of the anticodon can form H-bonds with more than one type of base located at the 3’ end of the codon (in the mRNA)

21
Q

How is aminoacyl-tRNA made?

A

“charging”: adding the amino acid to the tRNA to create an aminoacyl-tRNA (20 different versions for 20 different amino acids)

22
Q

What are ribosomes composed of?

A

The large subunit made of rRNA, proteins, and contains a peptidyl transferase center for formation of peptide bonds.
The small subunit is pretty much the same except it has a decoding center where charged tRNAs read and decode the codon of mRNA.
- Each subunit is seperate in cytoplasm, but together on mRNA
- Eukaryotic ribosomes are bigger

23
Q

What are the tRNA binding sites of ribosomes?

A

A. Aminoacyl: binds to the tRNA carrying the next amino acid to be added
P. Peptidyl: binds to the tRNA attached to the growing peptide chain
E. Exit: binds to the tRNA that carried the previous amino acid added

24
Q

Describe translation initiation.

A

An initiation complex (ribosome, mRNA, initiator tRNA) is formed after binding to methionine.
- Initiator tRNA brought to P site of small ribosome subunit (needs GTP)

  • tRNA + small subunit complex recruited to 5’cap of mRNA and scans 5’-3’ until first AUG
  • Complementary base pairing between initiator tRNA anticodon and mRNA start codon
  • Large subunit binds to small subunit to form initiation complex, which is now ready to accept first tRNA to A site
  • GTP hydrolyzed to GDP, translation begins now
25
Describe translation elongation.
- Correct aminoacyl tRNA loaded to A site by elongation factor - Peptidyl transferase in large subunit forms peptide bond between carboxyl group of growing peptide and the amino group of amino acid in A site - Ribosome moves and tRNA with polypeptide shifts from A to P site, uncharged tRNA moves from P to E - Next codon of mRNA is now in the A site, next aminoacyl tRNA can be loaded by elongation factor
26
Describe translation termination.
Releasing a completed polypeptide from the ribosome. - 3 termination codons (UAA, UAG, UGA) - Recognized by release factors, not tRNA - When ribosome reaches stop codon, release factor binds to A site and stimulates peptidyl transferase to cleave polypeptide from the P site - Ribosome subunits separate and detach from mRNA and the empty tRNA and release factor also separate
27
What are the two types of posttranslational regulation of proteins?
- Phosphorylation: addition of a phosphate group to a protein by kinase can activate or inhibit the proteins activity (phosphatases removes enzymes from phosphate) 2. Ubiquination: addition of ubiquitin molecules to proteins target them for destruction by the proteasome
28
What is epigenetics?
Changes in gene transcription that occur without changes to DNA sequence
29
What are some examples of epigenetic modifications?
- Histone acetyltransferase add acetyl groups to histone tails. This increases gene transcription and loosens chromatin - Histone deacetylases remove acetyl groups. This decreases gene transcription by compacting chromatin Together, these make up the histone code, which impacts transcription of genes
30
What does abundance of a protein depend on?
Translational regulation: control of protein synthesis Posttranslational regulation: control of protein abundance and activity - Abundance of protein depends on its rate of synthesis (translation) and rate of degradation (posttranslational)
31
What does activity of a protein depend on?
Depends on posttranslational modifications
32
So what does the expression level of a gene depend on?
Abundance and activity of the protein encoded by the gene