Proteins synthesis & genetic code 01 Flashcards

1
Q

How much energy in a cell accounts for protein synthesis?

A

80% of cell’s energy

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2
Q

What is body wasting?

A

Muscle-wasting (glu, aa) and subcutaneous fat loss (FA, energy, metabolites)

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3
Q

What is Marasmus starvation?

A

total calorie under-nutrition

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4
Q

What is Kwashiorkor?

A

Protein malnutrition, only in children eating food ok or high in calories but low in protein.
-> distorted serum aa composition, distorted liver aa pools, B-lipoprotein, albumin (edema)

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5
Q

What is are some common protein synthesis inhibitors /toxins?

A
  1. Alpha amanitine: RNA Pol II inhibitor
  2. Ricin: binding to the 60S subunit
  3. Diphteria: catalyzes the ADP-ribosylation of, and inactivates eEF2
  4. Trichothecene mycotoxins: problems w/rapidly growing tissues.
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6
Q

What are the 2 biological languages?

A
  1. The nucleotide language

2. The aa language

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7
Q

What are 3 important implication of the protein postulates?

A
  1. There is a genetic code
  2. RNA copy (mRNA) carries the code
  3. There is an apparatus (ribosome & tRNA) for translating the code.
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8
Q

What is the nature of genetic code?

A

a. 4 nucleotides
b. 20 letters in amino acid code
c. continuous code, nonoverlapping

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9
Q

What are the start and stop codons?

A

Start: AUG (Met)
Stop: UAA, UAG, UGA

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10
Q

What are some important characteristics of the genetic code?

A
  1. The code is triplet, non-overlapping
  2. Unambiguous (1 specific codon = 1 specific aa)
  3. Degenerate (1 specific aa = 1+ specific codons)
  4. Not universal
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11
Q

What are the 4 major steps of protein synthesis?

A
  1. Initiation: ribosome is assembled on mRNA
  2. Elongation: aa is brought to ribosome and it’s joined to nascent chain. Entire assembly then moves 1 position along mRNA
  3. Termination: at stop codon, no aa to add. Polypeptide is released from ribosome
  4. Disassembly: a special factor binds to the ribosome to release mRNA and tRNA.
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12
Q

What are the 3 exceptions to the 1 codon = 1 aa rule?

A

AUG: Methionine and N-formyl methionine
UGA: selenocysteine and stop codon
UAG: pyrrolysine and stop codon

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13
Q

How are selenoproteins synthesized?

A

A selenoprotein mRNA has a SECIS structure, selenocysteine insertion sequence, that adopts a stem-loop structure. This motif directs the cell to translate UGA codons as selenocysteines. Selenium is an essential trace element.
*Selenoproteins: antioxidant defense (glutathione peroxidase), thyroid hormone metabolism, lymphocyte activation, myocyte regeneration.

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14
Q

What are the 2 exceptions to the code degeneracy rule?

A

Met and Trp are encoded by a single codon

*Degeneracy is only found in the 3rd nucleotide of the codon.

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15
Q

Why is it said that the genetic code is not universal?

A

-Some of the code words are changed in some organisms, specially in the mitochondria. -Variations are consistent with view that mitochondria are ancient prokaryotic organisms. -Mitochondria protein synthesis is more simila to prokaryotic protein synthesis than eukaryotic.

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16
Q

What did Crick proposed about tRNA:mRNA interaction?

A
  • He proposed that the interaction at the 3’ mRNA position was unusually loose.
  • Watson-Crick bp in first two positions, but third position allows to wobble off with a G-U bp.
17
Q

Where do we see ionsine “I”?

A
tRNAs often occurs in the anticodon of tRNAs. It can bp with U, C, and A in the wobble position.
->3' codon base /  5' anticodon:
           A     / U or I
           C    /  G or I
           G    /  C or U
           U    /  A or G or I
18
Q

What are the two rules about protein synthesis?

A
  1. mRNA is translated from 5’ to 3’
  2. Proteins are synthesized from N-terminus to the C-terminus
    * 5’ of mRNA encode the N-terminal part of the protein
19
Q

How is prokaryotic protein synthesis different from eukaryotic one?

A

In prokaryotes, protein synthesis is closely coupled to mRNA synthesis in space and time.
In eukaryotes, mRNA synthesis occurs in the nucleus and translation in the cytoplasm; they both occur in the cytoplasm in prokaryotes almost at the same time.

20
Q

What is the overall structure of the eukaryotic mRNA?

A
5' cap (recruits ribosome)
AUG start codon
ORF (monocystronic)
Stop codon
Poly-A tail- 3'
21
Q

What are the “ingredients” for protein synthesis?

A
  1. Aminoacylated tRNAs
  2. Ribosomes
  3. mRNA
    * Ancillary protein “factors”
    * A special tRNA for initiation
22
Q

What is the structure of tRNA?

A
  • Cloverleaf structure folded to yield an “L” shape
  • Unusual nucleosides due to post-translational modificatiosn (pseudouridine, ribothymidine)
  • Phosphorylated 5’ terminus
  • 3’- OH-ACC, where amino acid is attached
  • 3 nucleotides in bottom loop form the anticodon
  • 4 loops: DHU, anticodon loop, variable, TΨC
23
Q

What is the ribosomal subunit fo euk/prokaryotes?

A

Each ribosome has 2 ribonucleoprotein subunits

a) Prokaryotes: 70S = 50S + 30S
b) Eukaryotes: 80S = 60S + 40S
- Small subunit: decoding center
- Large subunit: peptidyl transferease center

24
Q

How can ribosomal RNA be used for diagnosis of infections?

A
  • Most abundant type of RNA in the cell
  • While structure has been well preserved, there has been substantial divergence of 1ry sequence
  • Using probes specific for the ribosomal RNA of pathogenic bacteria and fungi, it will soon be possible to improve differential diagnosis.
25
Q

What is the aminoacyl-tRNA?

A

tRNA to which its amino acid chemically bonded (charged). The aa-tRNA, along with some elongation factors, deliver the amino acid to the ribosome for incorporation into the polypeptide chain that is being produced