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Biochemistry > RNA: Protein Synthesis > Flashcards

RNA: Protein Synthesis Flashcards

0
Q

Usually double stranded

A

DNA

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1
Q

Stores genetic information, building blocks of DNA/RNA.

A

Nucleic acids

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2
Q

Usually single stranded

A

RNA

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3
Q

Three-letter code that specifies a particular AA found within mRNA. ex: 5’-AUG-3’

A

Codon

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4
Q

Basic unit of a protein

A

Amino Acid

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5
Q

Complimentary code for a codon found within tRNA. Ex: 3’-UAC-5’

A

Anti codon

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6
Q

A series of arranged codons which codes for an mRNA

A

Gene

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7
Q

A special type of RNA which codes for a protein

A

mRNA

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8
Q

Process of converting a nucleic acid(mRNA) into a protein product

A

Translocation

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9
Q

Multiple codons can code for the same Amino Acid. UUU, UUC both code for ________.

A

Degenerate. Phenylalanine.

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10
Q

A particular codon can only code for a single amino acid. GUU can only code for ________.

A

Unambiguous. Valine.

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11
Q

Genetic Code Characteristics

A

Unpunctuated, Non overlapping & Universal “UNU”

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12
Q

Genetic Code Characteristic: there is no overlap in reading codons

A

Non-overlapping

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13
Q

Genetic Code Characteristic: the genetic code is the same for all animal species

A

Universal

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14
Q

Genetic Code Characteristic: no punctuation exists between or within codons

A

Unpunctuated

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15
Q

Is the process of converting a coded message within a messenger RNA into a polypeptide structure. Include _________.

A

Protein synthesis. Translation.

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16
Q

Polypeptide structure

A

Protein

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17
Q

An adapter molecule. Bridges the gap between your mRNA & protein. Cloverleaf shaped. Each of this species holds a single _______.

A

Transfer RNA. AA.

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18
Q

Parts of tRNA: where the AA is attached

A

Acceptor arm

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19
Q

Parts of tRNA: recognition site for specific aminoacyl-tRNA synthetase. Rich in dihydrouridine.

A

D arm

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20
Q

Parts of tRNA: binds aminoacyl tRNA to ribosomal unit

A

Thymidine-Pseudouridine-Cytidine arm

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21
Q

Parts of tRNA: seven-letter code containing the anticodon

A

Anticodon arm

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22
Q

In tRNA Activation: special enzyme, ____________, bind specific AAs with their corresponding tRNAs, with the help of ____. AAs are attached via their _______ at the 3’ end of the tRNA with an _________, forming an _________.

A

Aminoacyl-tRNA synthetases. ATP. Carboxyl end. Ester bond. Aminoacyl tRNA.

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23
Q

Contains adenine & guanine

A

Purines

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24
Q

Contains thymine, cytosine & uracil

A

Pyrimidine

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25
Q

Phases of Translation

A

Initiation, Elongation & Termination

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26
Q

Translation Initiation Phase: Ribosomes dissociate into 40s and 60s subunits

A

Dissociation

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27
Q

Translation Initiation Phase: Delays reassociation, allows for other IFs to mingle with 40s

A

elF-3 & elF-1A

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28
Q

Translation Initiation Phase: elF-2 binds to

A

GTP

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29
Q

Translation Initiation Phase: elF-2 GTP complex binds to

A

Met-tRNA

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30
Q

Translation Initiation Phase: elF-2-GTP-met-tRNA complex binds to

A

40s

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31
Q

Translation Initiation Phase: eiF2 binds to GTP. elF-2 GTP complex bind to met-tRNA and elF-2-GTP-met-tRNA complex binds to 40s.

A

43S preinitiation complex

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32
Q

Translation Initiation Phase: mRNA binds to 43s preinitiation complex. Via __________________. Uses GTP. Cap-binding protein complex eIF-4F binds to the methyl cap. Cap only in eukaryotes.

A

48s initiation complex

33
Q

Translation Initiation Phase: mRNA binds to 43s preinitiation complex via

A

Methyl-guanosyl triphosphate cap

34
Q

Translation Initiation Phase: In 48 initiation comples, eIF-4F consists

A

eIF-4E & eIF-4G

35
Q

Translation Initiation Phase: In 48s initiation complex, this is a scaffolding protein

A

elF-4G

36
Q

Translation Initiation Phase: In 48s initiation complex, it is responsible for recognizing the mRNA cap. It is phosphorylated by ______ and ______ to enhance initiation. Its is bound by _____ to inhibit initiation.

A

elF-4E. Insulin & Mitogens. BP-1.

37
Q

Translation Initiation Phase: In 48s initiation complex, insulin and mitogens ________ BP-1, preventing it from binding to _______ (which would enhance initiation)

A

Phosphorylate. eIF-4E.

38
Q

Translation Initiation Phase: In 48s initiation complex, melts the secondary structure of the cap. The complex begins to scar for ____________. Purines at positions -3 and +4 of the AUG sequence.

A

elF-4A & elF-4B. Zosak concensus sequences.

39
Q

Translation Initiation Phase: 48s initiation complex binds to 60s subunit. elF-5 hydrolyzes the GTP. this uses GTP as energy source. To remove all initiation factors. And to reassociate 60s & 40s.

A

80s initiation complex

40
Q

Translation Initiation Phase: In 80s initiation complex, 48s initiation complex binds to

A

60s subunit

41
Q

Translation Initiation Phase: In 80s initiation complex, hydrolyzes the GTP.

A

eIF-5

42
Q

Translation Elongation Phase: elongation factor eEF-1a complexes with GTP. Complex binds with an entering aminoacyl tRNA. Charged aminoacyl tRNA then enters this site.

A

A-site Attachment

43
Q

Translation Elongation Phase: In A-site attachment, complexes with GTP

A

eEF-1a

44
Q

Translation Elongation Phase: a-amino group of the A-site aminoa cid attacks the carboxyl end of the growing P-site polypetide chain. Facilitated by __________, a ribozyme component of the 60s subunit.

A

Peptide Bond Formation. Peptidyltransferase.

45
Q

Translation Elongation Phase: P-site tRNA is removed from the P-site. ________ facilitates the transfer of A-site tRNA to the P-site. Hydrolysis of the GTP will move ______ along the ribosome.

A

Translocation. eEF-2 + GTP. mRNA.

46
Q

Translation Elongation Phase: Energy requirement for activation of tRNA

A

2 ATPs

47
Q

Translation Elongation Phase: Energy requirement for entry of aminoacyl tRNA into A-site

A

1 GTP

48
Q

Translation Elongation Phase: Energy requirement for translocation

A

1 GTP

49
Q

Translation Elongation Phase: Total Energy requirement

A

4 high energy phosphate bonds

50
Q

Translation Phase: Stop codons enter the A-site. Releasing factors eRF remove the growing polypeptide from the P-site tRNA. mRNA detaches from ribosomes. Ribosome complex dissociates into 40s and 60s subunits.

A

Termination phase

51
Q

Translation Termination Phase: remove the growing polypeptide from the P-site tRNA together with GTP & Peptidyltransferase.

A

eRF

52
Q

Translation Termination Phase: mRNA detaches from

A

Ribosomes

53
Q

Releasing factor for UAA & UGA

A

eRF-2

54
Q

Releasing factor for UAA & UAG

A

eRF-1

55
Q

Releasing factor for binding of GTP

A

eRF-3

56
Q

Happens after translation. To promote protein functionality. Include many processes.

A

Posttranslational Processing

57
Q

In Posttranslational Processing: Some viral proteins: long __________ are cleaved to provide specific proteins.

A

Polycistronic proteins.

58
Q

In Posttranslational Processing: prohormone is a single chain protein. ________ cleaves it into two polypeptide chains, forming the functional hormone.

A

Insulin. Protease.

59
Q

In Posttranslational Processing: ______ molecules are translated. Three of these molecules align themselves. Enzymes _______ and _______ specific AAs. Amino terminal peptides are cleaved off.

A

Collagen. Procollagen. Hydroxylates & Oxidizes.

60
Q

In Collagen life cycle, cleavage of extension peptides by

A

Amino/Carboxyproteinases

61
Q

Segue to protein targeting

A

Translation

62
Q

Multiple ribosome units translating the same mRNA are called

A

Polyribosomes/Polysomes

63
Q

Polysomes are located either in free _______ or within _____.

A

Cytosol. RER.

64
Q

Secretory Pathway occurs in the

A

ER

65
Q

Tags aberrant proteins

A

Ubiquitin

66
Q

Destroys aberrant proteins

A

Proteasome

67
Q

Changes in the nucleotide sequence of a given DNA segment

A

Mutation

68
Q

Purine to purine OR pyrimidine to pyrimidine

A

Transition mutation

69
Q

Purine to pyrimidine OR pyrimidine to purine

A

Transversion mutation

70
Q

Mutation: add something

A

Insertion mutation

71
Q

Mutation: remove something

A

Deletion mutation

72
Q

Mutation type: inherent degeneracy of the genetic code. CUC to _____.

A

Silent/Nothing mutation. CUG.

73
Q

Mutation type: An amino acid is replaced with another AA. CUC to

A

Missense mutation. CCC.

74
Q

Mutation type: A codon for an AA is replaced with a stop codon. Results in premature termination. (Truncated protein) UAU, UAC to

A

Nonsense mutation. UAA,UAG

75
Q

Mutation type: error in reading the code due to either insertion or deletion. Occurs since the code is read 3 bases at a time.

A

Frame-shift mutation

76
Q

Mutation types: change something “MSN”

A

Missense, Silent & Nonsense

77
Q

Mutation types: add something

A

Frame-shift

78
Q

Mutation types: remove something

A

Frame-shift mutation

79
Q

Protein synthesis changes as a response to environmental threats. Excess iron in the blood triggers the synthesis of ________, which binds excess Fe2+.

A

Protein synthesis dysregulation. Ferritin.

80
Q

Changes as a result of viral infection.

A

Protein synthesis

Biochemistry (20 decks)

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