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Biochemistry > RNA: Protein Synthesis > Flashcards

RNA: Protein Synthesis Flashcards

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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
Contains thymine, cytosine & uracil
Pyrimidine
25
Phases of Translation
Initiation, Elongation & Termination
26
Translation Initiation Phase: Ribosomes dissociate into 40s and 60s subunits
Dissociation
27
Translation Initiation Phase: Delays reassociation, allows for other IFs to mingle with 40s
elF-3 & elF-1A
28
Translation Initiation Phase: elF-2 binds to
GTP
29
Translation Initiation Phase: elF-2 GTP complex binds to
Met-tRNA
30
Translation Initiation Phase: elF-2-GTP-met-tRNA complex binds to
40s
31
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.
43S preinitiation complex
32
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.
48s initiation complex
33
Translation Initiation Phase: mRNA binds to 43s preinitiation complex via
Methyl-guanosyl triphosphate cap
34
Translation Initiation Phase: In 48 initiation comples, eIF-4F consists
eIF-4E & eIF-4G
35
Translation Initiation Phase: In 48s initiation complex, this is a scaffolding protein
elF-4G
36
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.
elF-4E. Insulin & Mitogens. BP-1.
37
Translation Initiation Phase: In 48s initiation complex, insulin and mitogens ________ BP-1, preventing it from binding to _______ (which would enhance initiation)
Phosphorylate. eIF-4E.
38
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.
elF-4A & elF-4B. Zosak concensus sequences.
39
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.
80s initiation complex
40
Translation Initiation Phase: In 80s initiation complex, 48s initiation complex binds to
60s subunit
41
Translation Initiation Phase: In 80s initiation complex, hydrolyzes the GTP.
eIF-5
42
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-site Attachment
43
Translation Elongation Phase: In A-site attachment, complexes with GTP
eEF-1a
44
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.
Peptide Bond Formation. Peptidyltransferase.
45
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.
Translocation. eEF-2 + GTP. mRNA.
46
Translation Elongation Phase: Energy requirement for activation of tRNA
2 ATPs
47
Translation Elongation Phase: Energy requirement for entry of aminoacyl tRNA into A-site
1 GTP
48
Translation Elongation Phase: Energy requirement for translocation
1 GTP
49
Translation Elongation Phase: Total Energy requirement
4 high energy phosphate bonds
50
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.
Termination phase
51
Translation Termination Phase: remove the growing polypeptide from the P-site tRNA together with GTP & Peptidyltransferase.
eRF
52
Translation Termination Phase: mRNA detaches from
Ribosomes
53
Releasing factor for UAA & UGA
eRF-2
54
Releasing factor for UAA & UAG
eRF-1
55
Releasing factor for binding of GTP
eRF-3
56
Happens after translation. To promote protein functionality. Include many processes.
Posttranslational Processing
57
In Posttranslational Processing: Some viral proteins: long __________ are cleaved to provide specific proteins.
Polycistronic proteins.
58
In Posttranslational Processing: prohormone is a single chain protein. ________ cleaves it into two polypeptide chains, forming the functional hormone.
Insulin. Protease.
59
In Posttranslational Processing: ______ molecules are translated. Three of these molecules align themselves. Enzymes _______ and _______ specific AAs. Amino terminal peptides are cleaved off.
Collagen. Procollagen. Hydroxylates & Oxidizes.
60
In Collagen life cycle, cleavage of extension peptides by
Amino/Carboxyproteinases
61
Segue to protein targeting
Translation
62
Multiple ribosome units translating the same mRNA are called
Polyribosomes/Polysomes
63
Polysomes are located either in free _______ or within _____.
Cytosol. RER.
64
Secretory Pathway occurs in the
ER
65
Tags aberrant proteins
Ubiquitin
66
Destroys aberrant proteins
Proteasome
67
Changes in the nucleotide sequence of a given DNA segment
Mutation
68
Purine to purine OR pyrimidine to pyrimidine
Transition mutation
69
Purine to pyrimidine OR pyrimidine to purine
Transversion mutation
70
Mutation: add something
Insertion mutation
71
Mutation: remove something
Deletion mutation
72
Mutation type: inherent degeneracy of the genetic code. CUC to _____.
Silent/Nothing mutation. CUG.
73
Mutation type: An amino acid is replaced with another AA. CUC to
Missense mutation. CCC.
74
Mutation type: A codon for an AA is replaced with a stop codon. Results in premature termination. (Truncated protein) UAU, UAC to
Nonsense mutation. UAA,UAG
75
Mutation type: error in reading the code due to either insertion or deletion. Occurs since the code is read 3 bases at a time.
Frame-shift mutation
76
Mutation types: change something "MSN"
Missense, Silent & Nonsense
77
Mutation types: add something
Frame-shift
78
Mutation types: remove something
Frame-shift mutation
79
Protein synthesis changes as a response to environmental threats. Excess iron in the blood triggers the synthesis of ________, which binds excess Fe2+.
Protein synthesis dysregulation. Ferritin.
80
Changes as a result of viral infection.
Protein synthesis

Biochemistry (20 decks)

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