Protein synthesis and sorting Flashcards

(39 cards)

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
chemical modification in bacteria so to return to normal function after translation
N-formyl group and Met are removed
26
chemical modification in eukaryotes so to return to normal function after translation
Met is removed
27
internal stretches of amino acids
removed to produce an active protein
28
two types of splicing
intermolecular and intramolecular
29
inteins
remove certain amino acid sequences from poylpeptides
30
cotranslational import
movement of the polypeptide across or into the ER membrane | -directly coupled to the translational process
31
post translational import
polypeptides which are destined to cell organelles, required a special targeting signal
32
molecular chaperones
facilitate protein folding and assembly
33
protein folding is accompanied by the formation of what?
disulphide bonds between Cys in the pp chain
34
unfolded protein response (UPR)
detects misfiled proteins and enhances pathways for protein folding
35
ER-associated degradation (ERAD)
recognizes misfiled proteins and exports them back to cytosol for degradtion
36
glycoproteins
proteins synthesized on rough ER
37
where does initial glycosylation take place?
ER
38
where does further glycosylation occur?
golgi complex
39
what is the default pathway for soluble proteins?
golgi complex- secretory vesicles | -move to cell surface and fuse with palm membrane for secretion from the cell