Protein synthesis and sorting Flashcards

1
Q

ribosomes

A

carry out the process of polypeptide synthesis

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2
Q

tRNA molecules

A

align the amino acids in the correct order

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3
Q

aminoacyl-tRNA synthetases

A

attach amino acids to their appropriate tRNA molecules

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4
Q

mRNA molecules

A

encode the amino acid sequence information

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5
Q

facilitate some of the steps of translation

A

protein factors

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6
Q

made up of two dissociable subunits that resemble rRNA and proteins

A

bacterial ribosome

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7
Q

(A) aminoacyl site

A

binds each newly arriving tRNA with its attached amino acid

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8
Q

(P) peptidyl site

A

where the tRNA carrying the growing polypeptide chain resides

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9
Q

(E) exit site

A

from which tRNAs leave the ribosomes after they have discharged their amino acids

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10
Q

what directs the order of amino acids in a polypeptide?

A

sequence of codons in mRNA

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11
Q

nuclear export signals

A

for transport of mRNA through the nuclear pores

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12
Q

start codon

A

first to be translated

-usually AUG

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13
Q

step 1 of translation in bacteria

A

IF1,2,3 and GTP bind to small ribosomal subunit

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14
Q

step 2 of translation in bacteria

A

aminoacyl tRNA and mRNA are attached and bind to small ribosomal units

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15
Q

step 3 of translation in bacteria

A

large subunit joins and complex resulting 70S ignition complex and GTP is hydrolyzed

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16
Q

tRNA met

A

imitator in eukaryotes that carries methionine

-doesn’t become formylated

17
Q

cap-binding initiation factor, eIF4F

A

recognizes the 5’ end of the mRNA

18
Q

kozak sequence

A

AUG, start codon sequence

19
Q

what must be attached to the start codon for the large subunit to bind to the complex and start initiating?

A

initiator tRNA met

20
Q

aminoacyl tRNA binding

A

the ribosome bringing a new amino acid

21
Q

peptide bond formation

A

links this amino acid to the growing polypeptide chain

22
Q

translocation

A

moving the mRNA 3 nucleotides ahead to bring the next codon into position for translation

23
Q

release factors

A

protein that recognizes a stop codon in the A site

24
Q

hydrolysis

A

releases the polypeptide

25
Q

chemical modification in bacteria so to return to normal function after translation

A

N-formyl group and Met are removed

26
Q

chemical modification in eukaryotes so to return to normal function after translation

A

Met is removed

27
Q

internal stretches of amino acids

A

removed to produce an active protein

28
Q

two types of splicing

A

intermolecular and intramolecular

29
Q

inteins

A

remove certain amino acid sequences from poylpeptides

30
Q

cotranslational import

A

movement of the polypeptide across or into the ER membrane

-directly coupled to the translational process

31
Q

post translational import

A

polypeptides which are destined to cell organelles, required a special targeting signal

32
Q

molecular chaperones

A

facilitate protein folding and assembly

33
Q

protein folding is accompanied by the formation of what?

A

disulphide bonds between Cys in the pp chain

34
Q

unfolded protein response (UPR)

A

detects misfiled proteins and enhances pathways for protein folding

35
Q

ER-associated degradation (ERAD)

A

recognizes misfiled proteins and exports them back to cytosol for degradtion

36
Q

glycoproteins

A

proteins synthesized on rough ER

37
Q

where does initial glycosylation take place?

A

ER

38
Q

where does further glycosylation occur?

A

golgi complex

39
Q

what is the default pathway for soluble proteins?

A

golgi complex- secretory vesicles

-move to cell surface and fuse with palm membrane for secretion from the cell