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52 Cards in this Set

  • Front
  • Back

transduction

transfer of info (dna) from phage to bacteria

transformation
acquisition of an inheritable trait by bacteria mediated by dna
'formation, 'found info

conjugation

transfer of dna by sex pili

diameter of DNA molecule

20 angstroms

how many bp per one turn (360 degrees)

10.5 base pairs per turn

bases sepperated by (distance. how many ang?)

3.4 angstroms

adenine - thymine has how many h-bonds?

two hydrogen bonds. C-G bonding has three

structural variation in dna determined by:

1. conformation of deoxyribose (different puckering of ring)


2. rotation about the bonds making up the backbones


3. free rotation about the C-1'-N-glycosyl bonds

What alters DNA structure from typical b-type DNA?

local sequences, effect of DNA binding proteins, and extent of supercoiling

A-form DNA:
occurs in dehydrated DNA fibers,
wider and shorter helix
A-form A-typical (atypical)
True / False : dsRNA forms A and B like structure
False: dsRNA only forms A-like structure

Linking number

number of times one strand of circular DNA winds around the other in a right-handed direction

Twisting number

number of turns of the watson crick double helix



bp / 10.5 = Tw

writhing number

number of turns of super helix
Lk = Tw + Wr
Topoisomerase I
requires no energy
makes single strand breaks
removes negative supercoils
changes Lk by one

Topoisomerase II

requires atp


makes double strand breaks


changes Lk by two


introduces negative supercoils

what direction is chain growth in dna synth?

always 5' to 3' which means strand is copied from 3' to 5'

what does DNA polymerase do?

catalyzes phosphodiester-linkage formation

[E. coli]



which polymerase is most commonly used?


describe it's activity

DNA polymerase III


heteroligomer containint 10 types of subunits


two core domains


clam assemblies for high processivity


proof-reading activity


3' to 5' exonuclease for if mistakes (rare)

Describe helicase activity

domains A1 and B1 bind single strand DNA


ATP binds, clft between domains close


A1 slides along DNA


ATP hydrolysis, cleft opens, pulls dna from B1 to A1.


repeat

Final steps in DNA synth

DNA polymerase I removes RNA primers and fills in gaps with dNTPs


DNA ligase closes the remaining nick

differences in DNA synth (replication) from proks to euks
Eukaryoes:
multiple origins of replication
replicons (replication unit/origin) only replicated once per cell cycle - licensing factors

Teleomeres

hundreds of tangem repeats of AGGGTT


one strand is g-rich at 3' end and is longer


forms loop


Teleomerase uses innate RNA to extend leading strand

transversion (type of mutation)

pyrimidine replace by purine or purine by pyrimidine

transition (type of point mutation)

purine for purine, pyrimidine for pyrimiding

Shortest lived RNA's?

mRNAs are short-lived. carry info directly to protein synth. Produced for each gene

tRNA

do not carry information


act as 'adaptors' to pair amino acids n codons


at least 1 tRNA for each of the 20 amino acids

rRNA

structural and enzymatic


component of ribosomes


catalyze synth of proteins

RNA polymerase (proks)

(prok) one type for all RNA classes


one strand of DNA as template


plymerizes ATP, GTP, CTP, and UTP in 5' to 3'


antiparallele to DNA template

DNA sense and antisense strands

template is antisense strand (used to direct RNA synth)


non-template is sense or coding strand

inhibition of RNA polymerase

Proks: rifampicin


proks and euks: actinomycin D

RNA polymerase (euks)

(euk) one type of RNA pol for each class of RNA (3 types)


9-11 subunits

sense strand numbering

first nucleotide of sence that is transcribed is position +1


nucleotide prior to start of transcription is -1



*neg numbers are 'upstream' of transcription start site

T/F: promoters have approx equal binding strength

False: Not all promotors are created equal in strength and frequency of binding by RNA polymerase

consensus sequence of prok promotor

two sequences of 6 nucs. -10 to -35. pribnow box TATAAT

consensus sequence of euk promotor

(euk) RNA pol II binds to TATA box (TATAAA) aka Hogness box

Sigma factors

catalytically assist polymerase in finding correct promoter site. dissociate from active enzyme and repeat

transcription factors (when/where needed?)

All euks need factors!


RNA pol II binding to TATA requires TATA factor


Binding to GC box require Sp1


Binding to CAAT box require CTF



Proks do not need transcription factors

enhancer sequence

can activate transcription


act upstream, downstream, within transcribed regions



eg: steroid receptor complex to glucocorticoid enhancer

synthesis of mRNA precursor steps

1. start of elongation phase (no primer, purine first, 5' to 3', RNA no Hbond to DNA)


2. cap 5' end: 7-methylguanylate


3. endonuclease sees AAUAAA, cuts precursor


4. addition of poly A tail (250 A to 3' end)

Rho protein

contains ATPase activity, fast, binds to 72 nucleotides on RNA, zips away and finds/stops RNA pol

rRNA generation

Precursor molecule, nucleotide modification (methyl groups and pseudouridine), cleavage = mature rRNA


to 18S 5.8S and 28S in mamals

split genes not in prokaryotes

eg procollagen gene contains 52 introns.

mechanism of splicing mRNA precursors

1. 2' OH of A breaks bond between upstream exon and 5' of intron


2. 3' OH of upstream exon b bond between upstream intron


3. exon 1 and 2 joined, intron lariat relased, transesterification

mRNAs read in what direction for translation

mRNAs read 5' to 3'

number of codons, and tRNAs

64 possible, 61 codons, less tRNAs due to wobble position

Translation of mRNA (prok vs euk)

Eukaryotes contain monocistronic mRNA


Proks contain polycistronic mRNA (many genes)

5 stages of protein synth:

1. loading: aminoacyl tRNsynthetases, one per each amino acid (no proof reading)


2. initation of polypeptide synth: IF3


3. elongation


4. termination. RF1 or 2 bind to A site, OH it

Maximum density of ribosomes on mRNA

1 ribosome per 80 nucleotides

Energy required for synth of N# of amino acids

sum = 4N ATPs/GTPs



prot of 300 amino acids long: 4*(300) = 1200 phosphates. 1200x7.3= 8760 kcal/mol

What causes spontaneous folding of proteins?

h-bonds, van der Waals, ionic, hydrophobic.


folding and processing of proteins?

1. spontaneous


2. molecular chaperones


3. post-translational modifications: amino, carboxy, or carbohydrate side chain attach