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AP Bio > chapter 10: gene expression > Flashcards

chapter 10: gene expression Flashcards

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AP® Biology flashcards Biology 101 flashcards
0
Q

why diseases occur

A

mutant phenotype arises from a change in the protein’s amino acid sequence

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1
Q

archibald garrod

A

an early 1900s physician who applied mendelian genetics to patients and proposed that one gene codes to one enzyme
“inborn error of metabolism” (genetically determined biochem disease)

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2
Q

one gene - one polypeptide hypoth

A

one gene codes for one polypeptide (although they dont have to)
(modification of te one gene on protein hypoth)

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3
Q

molecular bio

A

the study of nucleic acids and proteins, focusing on gene expressiob

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4
Q

to translate genes into proteins

A
  1. transcription: the info in a dna sequence is copied into a complementary rna seq
  2. translation: rna sequence creates amino acid seq of a polypeptide
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5
Q

messenger rna

A

travels from nucleus to cytoplasm to be translated into a polypeptide

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6
Q

ribosomal rna

A

catalyzes peptide bond formation between amino acids fo form a polypeptide

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7
Q

transfer rna

A

mediates between mrna and protein; can 1. bind to a specific amino acid and 2. recognize a specific seq of nucleotides in mrna through complementary base pairing; recognizes which base should be added next to polypeptide chain

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8
Q

requirements for transcription

A
  1. dna template
  2. nucleotide triphoephates (atp, gtp, ctp, utp)
  3. an rna polymerase enzyme
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9
Q

promoter

A

dna sequence that initiates transcription by binding to the rna polymerase. they tell rna polymerase:

  1. where to start
  2. which two dna strands to transcribe
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10
Q

transcription initiation site

A

on the promoter; where transcription begins

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11
Q

elongation

A

rna polymerase unwinds 13 base pairs of dna and begins ro add new nucleotides to the growing strand

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12
Q

termination

A

base sequences that specify where to terminate transcription

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13
Q

coding regions

A

expressed as proteins; usually continuous

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14
Q

introns

A

noncoding sequences in genes that interrupt the coding region

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15
Q

exons

A

the regions between introns on genes; they are still expressed

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16
Q

nucleic acid hybridization

A
  1. dna denatured by heat to break hydrogen bonds and separate the strands
  2. a probe (single stranded nucleic acid from another source) is incubated with the dna. if complementary, the strands will join through hydorgen bonding
    RESULT: a hybrid
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17
Q

rna splicing

A

removes introns and splices exons together

18
Q

consensus sequences

A
  • short stretches of dna that appear with little variation, despite the gene
  • at boundaries of introns/exons
  • bound by small nuclear ribonucleoprotein particles (snRNPS), ehich have complementary bases to the consensus sequence
19
Q

spliceosome

A

rna-protein complex that cuts the pre-mRNA, releases the introns, and joins the exons
RESULT: mature mRNA

20
Q

alternative splicing hypothesis

A
  • not all exons are inclided in every mRNA; some are spliced out
  • results in different mRNAs and diff polypeptides from a single gene
21
Q

5’ cap

A
  • added to the 5’ end of the pre-mRNA as it is transcribed
  • facilitates the binding of mRNA to the ribosome for translation and protects mRNA from being digested by ribonucleases (enzymes)
22
Q

poly A tail

A
  • added to the 3’ end of pre-mRNA
  • helps exit from nucleus
  • mRNA stability
23
Q

redundant code

A

many diff codons for each amino acid

24
Q

ambiguous code

A

***genetic code is NOT ambiguous

would mean that a single codon codes for diff amino acids

25
Q

silent mutation

A
  • genetic code is redundant

- no change in amino acid sequence

26
Q

missense mutations

A

change in amino acid sequence

27
Q

nonsense mutation

A

result in premature stop codon

28
Q

frame shift mutation

A

result in insertion or deletion

29
Q

how to ensure right protein is made

A
  1. transfer rnas (tRNAs) must chemically read each mRNA codon correctly
  2. tRNA must deliver the amino acid that corresponds with the codon
30
Q

tRNAs

A
  • specific to each of the 20 amino acids (when carrying it, the trna is “charged”)
  • bind to mRNA: rhe anticodon on trna is complementary to the mrna codon for the amino acid
  • trnas interact with ribosomes
31
Q

aminoacyl-tRNA synthetases

A

family of enzymes specific to amino acid/corresponding trna

32
Q

ribosome sites where trna can bind

A
  1. a (amino acid) site: charged trna anticodon binds to mrna codon
  2. p (polypeptide) site: trna adds its amino acid to the polypeptide chain
  3. e (exit) site: trna rests before picking up another amino acid and restarting
33
Q

fidelity function

A
  • ensures charged trna with correct anticodon binds to right codon on mRNA
  • hydrogen bonds will form
34
Q

initiation complex

A
  1. charged trna and small ribosomal subunit bind to mRNA
  2. small subunit moves slong mRNA until it reaches start codon
  3. anticodon binds to start codon
35
Q

peptidyl transferase activity

A
  • large subunit breaks bond between methionine and its tRNA in P site
  • large subunit catalyzes the formation of oeotide bond between methionine and anino acid
36
Q

release factor

A

protein that allows hydrolysis of bond between polypeptide chain and tRNA in p site
stops elongation cycle

37
Q

polyribosome/polysome

A

an assemblags of a strand of mRNA and its beadlike ribosomes + their growinf peptide chains

38
Q

posttranslational aspects of protein synthesis

A

proteins can be modified after translation (adding new chem groups that contribute to fuction of mature protein)

39
Q

signal sequence (aka signal peptide)

A

short stretch of amino scids thst indicates where in the cell the polypeptide belongs
(diff signals depending on where proteins are destined to go)

40
Q

proteolysis

A
  • modification of protein post translation
  • cutting of the polypeptide chain
  • some proteins are actually polyproteins (long polypeptides of distinct proteins) and can be cut into proteases
41
Q

glycoslation

A
  • modification of protein post translation

- addition of carbohydrates to proteins –> form glycoproteins

42
Q

phosphorylation

A
  • modification of protein post translation
  • addition of phosphate groups
  • change the conformstion of the protein, exposing binding site for another protein or active site for an enzyme
  • caralyzed by protein kinases: important in cell signalling

AP Bio (7 decks)

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