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Biochemistry > Translation > Flashcards

Translation Flashcards

1
Q

Translation of RNA into protein

A

Convert mRNA sequence to protein sequence, uses specific code, 4 bases, 20 amino acids, three bases for one amino acid, codon in mRNA matches anticodon in tRNA

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2
Q

Start codon

A

AUG (ATG in DNA)

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3
Q

Stop codons

A

UAG, UGA, UAA

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4
Q

Total tRNA

A

Code is degenerate but unambiguous, 61 codons for amino acids, 3 stop codons, <61 tRNAs required

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5
Q

Reading the code

A

Start codon (AUG) sets the reading frame, each codon read in sequence, each signifies one amino acid or stop codon

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6
Q

Point mutations

A

Change of base pair, missense, nonsense, null, silent, can occur through DNA replication mistakes, repair mistakes, chemically altered base that mispairs

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7
Q

Deletion mutation

A

Removal of one or more bases, can occur through intercalating chemicals, DNA polymerase slips, mobile genetic elements

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8
Q

Insertion mutation

A

Addition of one or more bases, can occur through intercalating chemicals, mobile genetic elements

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9
Q

Frameshift mutation

A

Deletion or insertion of a number of bases that cannot be divided by three, occurs by intercalating chemicals, mobile genetic elements

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10
Q

Inversion mutation

A

Inversion of a sequence of bases (may cause frame shift), caused by mobile genetic elements

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11
Q

Silent mutation

A

A change that specifies the same amino acid

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12
Q

Missense mutation

A

Change that specifies a different amino acid

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13
Q

Nonsense mutation

A

Change that produces a stop codon

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14
Q

Consequences of frameshift mutation

A

Insert or delete bases, not a multiple of three, normal protein sequence before, completely changed after site of mutation, usually leads to premature termination by new stop codon in new reading frame

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15
Q

Splice site mutations

A

May decrease splicing efficiency, may alter splicing, inserting sequence from intron into mRNA or cause exon skipping, loss of one or more exons

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16
Q

Large insertions or deletions

A

Can remove large portion of the gene or entire gene, or interrupt gene with insertion

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17
Q

Triplet repeat expansion

A

Proteins with long run of same codon, may increase number of repeats with time, at some length repeat interferes with protein function and/or production

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18
Q

Amino acids and tRNAs

A

Amino acid is attached to specific tRNA by unique aminoacyl-tRNA synthetase, recognition site on tRNA varies for each, one aminoacyl-tRNA synthetase for each tRNA

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19
Q

Aminoacylation

A

Aminoacyl-tRNA synthetase, amino acid attached to terminal adenine of CCA, initial step uses ATP to form intermediate, carboxyl group on amino acid is joined to 3’ carbon of adenine by ester bond, amino group free to be added to polypeptide chain

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20
Q

Error correction

A

Incorrect amino acid is identified, transferred to editing site and removed, tRNA can be charged with correct amino acid

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21
Q

Initiation of translation

A

mRNA associates with small ribosomal subunit (30S/40S), charged met-tRNA binds to initiation factor and large subunit (50S/60S), components associate producing functional ribosomes, requires ATP and GTP hydrolysis for energy

22
Q

Prokaryotic protein factors in initiation of translation

A

IF-1, IF-2, IF-3

23
Q

Eukaryotic protein factors in initiation of translation

A

eIFs (eukaryotic initiation factors)

24
Q

Translation elongation

A

Amino acids are added to the carboxyl end of the growing polypeptide, delivery of aminoacyl-tRNA is directed by elongation factors, peptide bond formation is catalyzed by peptidyl transferase

25
Q

Elongation factors

A

EF-Tu (eEF1a bound to GTP), EF-Ts (eEF-1b), requires GTP

26
Q

Peptidyl transferase

A

Not a protein, is a ribozyme, enzymatic activity is associated with large ribosomal subunit (50S or 60S)

27
Q

Steps in elongation

A

Charged aminoacyl tRNA arrives at the aminoacyl (A) site, adjacent to previous tRNA in the peptide (P) site which is attached to the polypeptide chain, peptidyl transferase attaches the new amino acid to the chain, uncharged tRNA moves from P site to exit (E) site and is released, amino acid with the chain moves from A to P sites

28
Q

Translocation

A

Movement of the ribosome along the mRNA molecule, causes the net movement of the peptidyl-tRNA from the A site to the P site, uncharged tRNA is moved from the P to the E site where it is released

29
Q

Requirements for translocation

A

Requires EF-G (eEF2), GTP

30
Q

Termination of translation

A

Termination at first in frame stop codon, no tRNA with complementary anticodon, release factors bind, peptidyl transferase hydrolyzes the bond between polypeptide and final tRNA, ribosome subunits dissociate, release mRNA

31
Q

Polysomes

A

Each mRNA can associate with more than one ribosome, faster translation, as one ribosome translocates away from the 5’ end, another can be recruited

32
Q

Prokaryotic fMet tRNA

A

Initial methionine in prokaryotes does not have free amino group, formyl transferase enzyme adds formyl group, resembles peptide bond, removed later by another enzyme

33
Q

Post-translational modification

A

Proteins can be modified after synthesis, various groups can be added to specific amino acid residues, modify function, activity, or help target protein to sub-cellular compartments

34
Q

Carboxylation

A

Glutamate, ex- coagulation cascade

35
Q

Hydroxylation

A

Proline, lysine, ex- collagen stability

36
Q

Phosphorylation

A

Serine, threonine, tyrosine, ex- enzyme activity

37
Q

Glycosylation

A

Serine, asparagine, ex- secretion, membrane

38
Q

Fatty acylation

A

Ex- membrane anchor

39
Q

Prenylation

A

Ex- membrane anchor

40
Q

ADP-ribosylation

A

Ex- enzyme activity

41
Q

Collagen assembly

A

Procollagen is post-translationally modified, hydroxylation of proline and lysine, glycosylation, triple helix forms and is stabilized by hydrogen bonds from hydroxyproline and hydroxylysine residues

42
Q

Osteogenesis imperfecta

A

Caused by defects in collagen assembly or stability due to missense mutations, defects in post-translational modifications

43
Q

Protein targeting

A

Proteins for secretion, membranes, organelles are often modified in ER and Golgi, synthesized by ribosomes of rough ER

44
Q

Ribosomes of rough ER

A

Signal peptide of nascent protein binds signal recognition particle (SRP), docks with receptor on ER, protein enters ER lumen via pore, can be modified and enter secretion pathway

45
Q

Lysosomal enzymes

A

Enzymes to degrade large molecules, modified with mannose-6-phosphate in Golgi, without M6P enzymes go to secretory vesicles and out of cell

46
Q

I-cell disease

A

Lack of phosphotransferase activity, lysosomal enzymes leak out of cells, lysosomes filled with debris (inclusion bodies), serious health effects

47
Q

Streptomycin

A

Inhibitor of protein synthesis, binds to the 16S rRNA of the 30S subunit, inhibits translation initiation

48
Q

Tetracycline

A

Inhibitor of protein synthesis, binds to the 30S ribosomal subunit, blocks binding of the aminoacyl-tRNA to the A site of the ribosome, many bacteria are resistant

49
Q

Chloramphenicol

A

Binds to 50S ribosomal subunit, blocks binding of amino acid on aminoacyl-tRNA, blocks peptidyltransferase activity, can inhibit mitochondrial activity, only used in serious conditions

50
Q

Erythromycin

A

Binds to 50S ribosomal subunit, prevents translocation

Biochemistry (18 decks)

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