Week 7 Flashcards

1
Q

What is the central dogma?

A

The process of going from DNA to RNA to proteins using transcription and translation

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2
Q

What differentiates DNA and RNA in structures?

A

RNA has a 2’ OH group, RNA is single stranded vs DNA which is double stranded

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3
Q

Primary structure

A

The amino acid sequence

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4
Q

Secondary structure

A

The local folding of alpha helices/beta pleated sheets

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5
Q

Tertiary structure

A

Overall folded shape of the amino acid chain

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6
Q

Quaternary structure

A

The shape of multiple tertiary structures together

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7
Q

Stop Codons

A

UGA, UAA, UAG

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8
Q

What is the start codon?

A

AUG

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9
Q

Reading frame

A

AUG to stop codon

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10
Q

Intragenic suppression

A

How a gene can still function if one mutation cancels another in the same gene (frame restoration)

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11
Q

Frameshift mutations

A

A single-base deletion/insertion that shifts the reading frame of the amino acid sequence

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12
Q

tRNA

A

74 to 95 nucleotides long, carries a specific amino acid, have anticodons

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13
Q

How was the amino acid code decoded?

A

Used radioactively labelled amino acids. As translation occurred, the mixture was poured through a filter, allowing only tRNAs that had the correct amino acid stick to the filter

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14
Q

Transcription

A

Going from DNA to RNA, uses Uracil instead of Thymine, still complementary base pairing

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15
Q

Synthesis occurs in what direction?

A

5’ to 3’

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16
Q

RNA polymerase

A

Enzyme used to catalyze transcription

17
Q

Promoter

A

DNA sequence near the beginning of genes that tell RNA polymerase where to start transcription

18
Q

Terminators

A

Sequence in RNA product that tells RNA polymerase where to stop transcription

19
Q

Transcription Initiation

A

Sigma factor recognizes the promoter on DNA, and RNA polymerase binds (which releases the sigma factor)

20
Q

Transcription Elongation

A

RNA polymerase makes its way along the chain, complementary base pairing rNTPs

21
Q

Rho-dependent Transcription Termination

A

Rho protein binds to RNA sequence that is C-rich pulls mRNA away from polymerase

22
Q

Rho-independent Transcription Termination

A

G/C rich section in RNA, creates hairpin loop, RNA polymerase is released

23
Q

Differences between prokearyotic genes and eukaryotic genes

A

Prokaryotes cannot rearrange genes like eukaryotes rearrange exons, different post-translational modifications

24
Q

G’ cap

A

Adding a methylated G at 5’ end of eukaryotic mRNA to prevent degradation

25
Poly A Tail
3’ end of eukaryotic mRNA, also prevents degradation, helps with translation
26
RNA splicing
Rearranging of exons by removing introns (alternative splicing) - Cuts at 5’ site, which folds over, cut at 3’ site EX: Dystrophin gene has MANY introns
27
Translation
Converting RNA to protein
28
Prokaryotic Translation Initiation
Shine-Dalgarno sequence is recognized by complementary sequences in rRNA (upstream of initiation codon). Initiation codon signals addition of tRNA with Methionine, which binds the two subunits of the ribosome together (previously just small subunit, Met is in P site
29
Eukaryotic Translation Initiation
Small subunit binds to G’ cap instead
30
Translation Elongation
- Elongation factors bring next tRNA over into A site, peptidyl transferase creates the peptide bond between the two amino acids - Ribosome moves along mRNA, Met moves to E site, more tRNA appears, etc
31
Translation Termination
Stop codon is reached, release factor binds to A site, polypeptide is released
32
Wobble
Where some tRNAs are able to recognize more than one codon (has specific rules)
33
Structure of the ribosome
- Three sites, Aminoacyl site (A), Peptidyl site (P), Exit site (E) - Made of large and small subunit - Protein and rRNA
34
Polyribosome
Several ribosomes translating the same mRNA
35
Post-translational processing
Cleavage: cutting protein into smaller polypeptides Adding a phosphate group, etc