Protein Synthesis and sorting Flashcards

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1
Q

What is Translation?

A

mRNA is decoded in a ribosome to produce a specific amino acid chain, or polypeptide

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2
Q

What are the five major components are involved in translation?

A

Ribosomes, tRNA molecules, Aminoacyl-tRNA syntheses, mRNA molecules and Protein factors

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3
Q

attach amino acids to their appropriate tRNA molecules

A

Aminoacyl-tRNA synthetases

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4
Q

encode the amino acid sequence information

A

mRNA molecules

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5
Q

Protein factors function as what?

A

facilitate some of the steps of translation

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6
Q

Made of two dissociable subunits; large subunit and small subunit
Each subunit self-assembles from rRNA and proteins
come together only when binding mRNA

A

The bacterial Ribosome

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7
Q

How many and what are the binding sites of a Ribosome?

A
3 tRNA (A aminoacytl site, P peptidl site, E Exit site)
mRNA binding site
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8
Q

an adaptor that binds both a specific amino acid and the mRNA sequences that specify the amino acid

A

tRNA

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9
Q

Once amino acid is attached to tRNA it is called

A

amino acyl tRNA

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10
Q

Messenger RNA Brings what Information to the Ribosome

A

Polypeptide Coding

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11
Q

mRNA is exported to the cytoplasm via binding to mRNA-binding protein that contains amino acid sequence …

A

nuclear export signals (NES) for transport through the nuclear pores

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12
Q

Start codon where translation starts (N-terminus of polypeptide) and the stop codon is where

A

where translation ends (C-terminus of polypeptide (UAG, UAA, UGA)

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13
Q

Initiation of translation in bacteria: Assembly of the 70S translation initiation complex occurs in ___ steps

A

3

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14
Q

Step 1: initiation of translation

A

Three initiation factors (IF1, IF2 and IF3) and GTP bind to the small ribosomal subunit

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15
Q

Step 2: initiation of translation

A

The initiator aminoacyl tRNA and mRNA are attached and bind to the small ribosomal unit
initiator tRNA is tRNA that carries an N formylmethionine→ tRNAfMet

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16
Q

Step 3: initiation of translation

A

The large subunit joins the complex resulting 70S initiation complex and GTP is hydrolysed

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17
Q

The start codon in eukaryotes and archaea specifies

A

methionine rather than N-formylmethionine

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18
Q

After binding to mRNA, the small ribosomal subunit begins translation at the

A

first AUG triplet it encounters

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19
Q

a common start sequence is ACCAUGG called a

A

Kozak sequence, the entire thing is a start codon

20
Q

Chain elongation involves what three steps

A

Aminoacyl tRNA binding
Peptide bond formation and
Translocation

21
Q

Termination: A stop codon goes to the A site and recognized by

A

Release factors

22
Q

releases the polypeptide

A

Hydrolysis

23
Q

Post translational processing

A

Must be chemically modified before they perform their normal functions

24
Q

In bacteria which two groups are removed during Post translational processing

A

N-formyl group and the Met are removed

25
Q

In eukaryotes which group is removed during Post translational processing

A

Met at the N-terminis

26
Q

Some enzymes synthesize as

A

inactive precursors, and must be activated by removal of specific sequences at one end or the other

27
Q

Internal stretches of amino acids are

A

removed to make an active protien

28
Q

Chemical modifications of individual amino acid groups by what three ways

A

methylation, phosphorylation or acetylation

29
Q

Ploypeptides may undergoto to prosthetic groups

A

glycosylation or binding

30
Q
  • inteins are removed from a one or more polypeptides
  • Resulting segments create a continuous polypeptide chain
  • can be intramolecular or intermolecular
A

Protein Splicing

31
Q

What are the two types of protein targeting and sorting?

A

Cotranslational and Posttranslational import

32
Q

Posttranslational

A

after translation is completed, the polypeptides which are destined to cell organelles. Requires presence of special targeting signals

33
Q

movement of the polypeptide across or into the ER membrane is directly coupled to the translational process

A

Cotranslational import

34
Q

facilitate protein folding and assembly

A

Molecular chaperones

35
Q

Folding is accompanied with formation of disulfide bonds between

A

Cys in the pp chain

36
Q

Improperly folded proteins can activate

A

several types of quality control mechanisms

37
Q

Unfolded protein response (UPR)

A

detect misfolded proteins and enhance pathways for protein folding

38
Q

recognizes misfolded proteins and exports or ‘retranslocates’ them back to cytosol for degrdation

A

ER-associated degradation (ERAD)

39
Q

Proteins Released into the ER Lumen Are Routed to the

A

Golgi Complex, Secretory Vesicles, Lysosomes, or Back to the ER

40
Q

Most proteins synthesized on rough ER are

A

glycoproteins

41
Q

The initial glycosylation takes place in the __ as the polypeptide is being synthesized

A

ER

42
Q

Default pathway:

Soluble proteins move from the Golgi complex to

A

Secretory vesicles

43
Q

The other major group of polypeptides is destined to become

A

integral membrane proteins

44
Q

The completed polypeptide chain remains embedded in the ER membrane and then

A

can be targeted to its proper destination

45
Q

Posttranslational import into organelles that are

A

not part of the endomembrane system

46
Q

Proteins imported into organelles after completion of translation are synthesized on

A

free ribosomes and released into the cytosol