2007 MT3 key

2007 MT3 key - Last Name: K I , First Name: Lab (day and...

Info iconThis preview shows pages 1–5. Sign up to view the full content.

View Full Document Right Arrow Icon
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Background image of page 2
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Background image of page 4
Background image of page 5
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: Last Name: K I , First Name: Lab (day and time]: , Tats: BISC 32D Midterm 3: Nov. 14: Elli]? Please print your last and first name on 1rer},r page. (1 pt deduction for each violation} Answers in pencil or with 1whiteout will NOT he re-graded! I. (It) pts} 1|When conservative site—specific serine—type recombinases cause recombination in vivo between two double stranded DNA sequences, hon.r does this type of reeomhinase initiate {start} the events leading to the final recombination? Answer: These recomhinases first cause a nick in each strand of each of the duplex DNAs t I'out nicks. total} that are in register with {jach when Dog-i» flfl‘i' fhPIri-t'onf drifter} Gr {imply Hzm'i‘ iiié’ré’ til-V8 q-f'u'litti of 91W midi-“‘7 ‘. 410M 1‘ P9." {Drier réiceflea'qwtt’ho and; f hm Hawaii g-F Uri/fig i a M?- Iiaur titt‘t'fi’t‘s(timer:er.,1K in?!” at +90” “will W hmbé affirm! arm #3: Only :aKE‘f from ,4,ng nr flare fimJE’A deem" .3} Matt; are m+ fiayglfirf’oi. W “"1 poms not oar wt. ~40 I I. _‘ Mf’fl‘l‘ldoéHgE-ngglfgafiafi; d5. 6’; fag? {chef/£533. S Ii? 2. If l D p E s nees involved in ereat1ng d ons in double stranded DNA? Answer: The ere gene codes for a reeomhinase protein ‘WhiCh removes douhle stranded DNE‘t between two 1o_x sequences {including the two Io_x sequences}. L} ‘ Poe; ("113+ €><piotn "HM? {def/Hon af‘ 06.5% -Inrsrrecily QXPiains ihe {Madden 04" CFE- 9’ (mi eyPlaio Hie-i Hg in): fecbdencgr are tor-L, ‘ Dale; fireflilfl CU'i' €£+r offlind 1‘ 4‘ . gust at explaqu i’hfi {3aneiirfi at are MW” _3 * ~ rs coo-12:3; me full" if” . WE’fih—tnnln—Hfim - 1 ' it l3" olgfgfififl- . I x } tiin‘; their Cre {leader or Caulfl Jane Dieter“ was Exp! I I ‘1 t #Pntisqifi +L1lr-‘i tit} [J LL FE? Euwbtfiafl? 53F Pruifrfig L} I 011E} fibril Know CrE ‘iixfi Lfinbtpajfil/bu'i NIL-I“; {2:1 (1 reroute-mt» o tiwwrdn - Thank; lLst link is a reevaasflare. H5 oi" -—-| First Name: Page 2 3. {Hi pts} {at 1dr'ita! neeurs iirst at a target DNA sequence prietr tt) itttegt'ttlidtt Oran [S or TN eietttettt at the target site? .-"'-.nst'-.er: [:I} Staggered DNA nieks appear uernss [hath strands are cut} the dttttble stranded target Hart. sequenee ' I; {7 DNA “at; affeaiFiE}Ffig:| 501% ar€ aw‘é' [h] "it"iten :1 prttkaryntie transparent] {i5 pr TN} “jumps” to a new site {target} and integrates there. why does the target sequence appear. as direct repeats. at each end eitlte new integrated transpn stn't'.’ _-"rttst.xer: {h} .-"'tii.t.T a transpasase tar. an integrase} lands at a target site an duplex thisr‘t and ereates staggered nieks tune [in eaeit 1351.31 strand at this site]. li'ttiitiflimitlg. square-ended duplex HIE-"t trtthsppsun inserts itself. teat-int:- single stranded Tiffi‘rs‘at eaeh end. The gaps are tilted it} HEP-t repair and ligation. creating t Ireet repeats at ease 'I end tritlte trattsptrsun. 2}; e . TWS/ygjajfl av“ t'fl'iifjrfir Smite sand jaw/95' rifles thievétWE-f DNA Fflzmiii” HM @frfiwt (Mi Vflmfiifib “5/” '41. [191115]: ‘t'erjt' brieflxt. ittrtx' are LTRS inv ed in Il'fll‘lSpDSitiDt'l Oran integrated rett'atranapeaen'? .-"tttst'-.er: 'I'rattseriptiflrt fliifl t'ett‘dtt'altspdsnn starts within théliett hand HR and steps within the right hand ifl‘R. 'i'hen. alter emu-erstan et'a transerihed t'ira] Rita's-t. strand intrr duuhle stranded ]}N.-"'t_ the t'estul'ed LTR ends tit-tins DNA allew integratian. t-‘ia an FIFE—binding transprrsase [integraset inter a new eitrdntastmta] target site. (cit—tarsyd Am 7,9155 ficirfl‘i rflgareffra Vt 3 {0 t5} 7 “Starr’s L76 _ Wiflfi Q - t /9 5 T5158; ELJ‘fl} 7th First Name: Page 3 5. {112} pts] After a PLIVRI sequence pairs with an R21 sequence at the beginning cfa specific VJ joining in a B Iympheeyte. briefly. what are the next steps in allewing VJ jcining tn finallyf cecur‘? H Answer: {£161 41252 hctcrndgeric ein deletes the i enin double stranded DNA. ‘- includin r R] and R2, the PLW and J ends tentpnrerilv hairpini and then there is VJ jeining “’le hunks to J}. I } 1 b. [10 pts} Dining RNF’L splicing, hew does the branch point in a pre—mRNA intren participate in fanning a lariat structure? (What are the proteins, RNPs, splice sitE:(E}, etc. involved in ferming s Isriat?} Ll Answer: An SR retein binds to an E5 " -' se ne 'e, LilsnRN binds to the 5' sp ec siteI BPB retein and UanRNP bind to the branch cin en the severed 5‘ end of t e int Inna. connects via a 5'—2* cennectmn tn the A in the branch cint within the intrcn. First Name: Page 4 e” 5’ 'i'. {I I1]I pts} How do SR proteins {a} control alternative pre—mRNA splicing and (b) initiate (start) spliceosomal splicing within pro—InRNi’t strands?I {It is not necessary to describe the entire assembly of new spliceusomes.) 3 6 .. a +5 I 4: Answer: {a} Phosphoryiation 'dit‘lierent serines within SR proteins controls alternative & Pi":- splicing by regulating whether a s ecil'ie SR rotein will hind with a particular ESE {or 1513} sequence. {b} SR proteins bind to ESE sequences within esons on pre—mRNr‘t strands an emitsnRNFs to hecome'attachcd to nearby 5' splice sites. 5' fry; E. [1U pts} __ {a} Where on tRNA molecules do aminoacyl synthetase enzymes (“charging" enzymes) attach 1'1 an amino acid‘:1 Answer: {at These enzymes attach an amino acid on the 3* end of the [RNA molecule (or. the answer could be:- on the [.‘Cr‘t end of the tRNAJ. 5 F_———-—_ 6' 45" {b} Considering the number of kinds of amino acids utilized in synthesizing proteins, what would be your best guess as to the minimum number of kinds ofaminoaeyl synthtase enzymes in most eukaryotic cells? Answer: (h) The number would likely be at least ELL since most organisms use 2U itinds ot' .-_——-—"" amino acids in protein synthesis. 5- t’f't I First Name: Page 5 s. [It] p15} {at} How does a eukaryetie 43$ ribosome complex participate in initiating [starting] synthesis oFthe amino terminal end ofa protein? Answer: {a} 'l'he_£_t_3_i~l complex scans the mRNA as it travels to find the correct AUG translation start eodon. (There. the 1505 ribosome subunit attaches. producing the 3GB cukaryotic ribosonte.) {b} How does the 433 ribosonie complex form? {It is not necessaryr to name the actual protein translation factors in describing these two processes} Answer: {b} Alter a 4GB snbtmit attaches at a CAP site, the 4% subunit picks up a number at translation initiating I'aetors. becomes a 433 complex. It). {lfipts} What effect does a translational frameshift mutation in a gene have on {a} the transcribed mRNA nucleotide sequence and (b) the translated protein amino acid sequence? at Answer: The frame-shifting deletion or addition oi‘ nucleotide base pairs in the DNA would have a con'esponding addition or deletion of bases in the mRNA. '3} Answer: [Tollinearly with the DNA. the amino acid sequence downstream {toward the carbons terminal end}. starting at the mutation site, would be different compared with the protein coded for by the wild type. non-mutated gene. ...
View Full Document

This note was uploaded on 09/12/2009 for the course BISC 320L taught by Professor Baker,aparicio during the Fall '07 term at USC.

Page1 / 5

2007 MT3 key - Last Name: K I , First Name: Lab (day and...

This preview shows document pages 1 - 5. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online