lQ interaction with E. coli RNA polymerase for antitermination Regions of E. coli RNA polymerase required for lQ-mediated antitermination in binding a » książka
lQ interaction with E. coli RNA polymerase for antitermination Regions of E. coli RNA polymerase required for lQ-mediated antitermination in binding a
ISBN-13: 9783639165814 / Angielski / Miękka / 2009 / 176 str.
lQ interaction with E. coli RNA polymerase for antitermination Regions of E. coli RNA polymerase required for lQ-mediated antitermination in binding a
ISBN-13: 9783639165814 / Angielski / Miękka / 2009 / 176 str.
(netto: 291,72 VAT: 5%)
Najniższa cena z 30 dni: 303,45
ok. 10-14 dni roboczych.
Darmowa dostawa!
Phage Q protein is a transcriptional antiterminator that is required for late gene expression from the pR' promoter when prophage decides to follow the lytic pathway. Q modifies Escherichia coli RNA polymerase (RNAP) at the early elongation stage. Once engaged, Q maintains itself as a subunit of the elongation complex throughout the elongation. Studies show that Q confers RNAP resistance to both intrinsic and -mediated terminators and less pausing. However, little is known about the interaction between Q and RNAP. In this study, the largest subunits ( and ') of RNAP were examined to map the Q binding site. A stronger binding was observed with than ', and the binding site was narrowed to 501-832. This region was further defined as small as 82 amino acids ( 600-681) that interacted with Q. In addition, 12 mutant RNAPs were isolated for a reduced Q antitermination within the potential Q binding regions, specifically near the main channel. These results propose that Q modifies the active center of RNAP for antitermination."
Phage λQ protein is a transcriptional antiterminatorthat is required for late gene expression from the pR promoter when λprophage decides to follow the lytic pathway. λQ modifiesEscherichia coli RNA polymerase (RNAP) at the early elongation stage. Onceengaged, λQ maintains itself as a subunit of the elongationcomplex throughout the elongation. Studies show that λQ confers RNAPresistance to both intrinsic and ρ-mediated terminators and lesspausing. However, little is known about the interactionbetween λQ and RNAP. In this study, the largest subunits (β and β) ofRNAP were examined to map the λQ binding site. A stronger binding wasobserved with β than β, and the binding site was narrowed toβ501-832. This region was further defined as small as 82 amino acids(β600-681) that interacted with λQ. In addition, 12 mutant RNAPswere isolated for a reduced λQ antitermination within the potentialλQ binding regions, specifically near the main channel. Theseresults propose that λQ modifies the active center of RNAP forantitermination.
Czytaj nas na:
KrainaKsiazek.PL - Księgarnia Internetowa
