MARC Record from University of Toronto

LEADER: 02059nam 2200253 4500
001 AAIMQ95187
005 20050602151747.5
008 050602s2004 onc|||||||||||||| ||eng d
020 $a0612951871
039 $fws
100 1 $aDavidson, Toni.
245 10 $aTowards understanding the functions of the GroEL and ClpX chaperone systems in Escherichia coli.
260 $c2004.
300 $a128 leaves.
500 $aAdviser: Walid A. Howy.
502 $aThesis (M.Sc.)--University of Toronto, 2004.
506 $aElectronic version licensed for access by U. of T. users.
510 0 $aSource: Masters Abstracts International, Volume: 43-03, page: 0847.
520 $aMolecular chaperones are proteins that assist in folding, refolding, disaggregation, or degradation of other proteins in the cell. This thesis includes studies of two bacterial chaperones, GroEL, which mediates protein folding, and ClpX, which mediates protein unfolding and directs proteins for degradation by ClpP. GroEL has previously been implicated in the refolding of the multisubunit bacterial RNA polymerase (RNAP). I found that GroEL was not essential for the refolding of the alpha and o subunits of RNAP. Previous studies have indicated that the N-terminal Zinc Binding Domain (ZBD) of ClpX is involved in substrate recognition. Using degradation assays and competition studies, I found that the ZBD of ClpX is important for recognizing a certain set of substrates. Placement of an N-terminal tag on ClpX results in cleavage of that tag in the presence of ClpP and ATP. This suggests that a conformational change takes place in ClpX involving the ZBD.
590 $aMICR copy on microfiche (2 microfiches).$5CaOTU
653 $aChemistry, Biochemistry.
856 41 $uhttp://link.library.utoronto.ca/eir/EIRdetail.cfm?Resources__ID=94865&T=F$yConnect to resource
949 $aOnline resource 94865$wASIS$c1$i5402897-2001$lONLINE$mE_RESOURCE$rY$sY$tE_RESOURCE$u13/6/2005
949 $atheses masters$wALPHANUM$c1$i31761061901104$lMICROTEXT$mMEDIA_COMM$rY$sY$tMICROFORM$u13/6/2005$o.PUBLIC.