Author: Mark Steven Kainz
Publisher:
ISBN:
Category :
Languages : en
Pages : 356
Book Description
Transcription Antitermination Mediated by the Phage Lambda Q Protein
Author: Mark Steven Kainz
Publisher:
ISBN:
Category :
Languages : en
Pages : 356
Book Description
Publisher:
ISBN:
Category :
Languages : en
Pages : 356
Book Description
Transcription Antitermination Mediated by Lambdoid Phage Q Proteins
Author: Xianjie Yang
Publisher:
ISBN:
Category : Bacteriophage lambda
Languages : en
Pages : 446
Book Description
Publisher:
ISBN:
Category : Bacteriophage lambda
Languages : en
Pages : 446
Book Description
Mutational Analysis of Transcription Antitermination Mediated by Lambdoid Phage Gene Q Products
Author: Hwai-Chen Guo
Publisher:
ISBN:
Category : Bacterial proteins
Languages : en
Pages : 654
Book Description
Publisher:
ISBN:
Category : Bacterial proteins
Languages : en
Pages : 654
Book Description
Regions Of E. Coli RNA Polymerase Required For Lambda Q-Mediated Antitermination In Binding And Function
Author: Heeyoun Bunch
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
Book Description
Controlled gene expression in phage [lamda] is a model of transcription regulation which is mainly mediated by transcription factors to activate or repress E. coli RNA polymerase (RNAP). They switch appropriate genes on or off, determining the lysogenic or lytic pathway of progeny phages. Q is a [lamda] late gene regulator that exerts antitermination for products of the pR' promoter. Previous studies presented exciting aspects of [lamda]Q modification of RNAP which cause dramatic changes in the protein under certain conditions. RNAP engaged with [lamda]Q escapes a [sigma]-mediated promoter proximal pause and overcomes an intrinsic terminator downstream of the pR' promoter. In addition, [lamda]Q alters RNAP dynamics, aiding faster elongation, fewer pauses, and resistance to both the intrinsic and [rho]-dependent termination. Although [lamda]Q-mediated antitermination was characterized with previous works as described above, the mechanism by which [lamda]Q exerts antitermination is still unclear. In order to uncover this mechanism, this study attempted to answer the fundamental question of where [lamda]Q interacts with RNAP. First, the two largest subunits of RNAP were systematically dissected to map a [lamda]Q binding region on RNAP. The results suggested a clustered region of three fragments of [beta] and [beta]' for [lamda]Q binding, and as small as 82 amino acids ([beta]600-681) within this region were identified to bind to [lamda]Q. Second, a potential [lamda]Q binding region of RNAP proposed by a previous study was evaluated in this study. Although the region is located in the surface domain of [beta]600- 681, mutational analyses targeting the region demonstrated little [lamda]Q binding. Third, twelve RNAP mutants that reduce [lamda]Q-mediated antitermination were identified, and they suggested four spatial regions of RNAP as critical for [lamda]Q antitermination. Finally, one of the RNAP mutants, [beta]K1073G, presented altered function of NusA, a transcription elongation factor, in [lamda]Q-mediated antitermination at the intrinsic terminator, providing evidence of cooperation between NusA and [lamda]Q antitermination.
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
Book Description
Controlled gene expression in phage [lamda] is a model of transcription regulation which is mainly mediated by transcription factors to activate or repress E. coli RNA polymerase (RNAP). They switch appropriate genes on or off, determining the lysogenic or lytic pathway of progeny phages. Q is a [lamda] late gene regulator that exerts antitermination for products of the pR' promoter. Previous studies presented exciting aspects of [lamda]Q modification of RNAP which cause dramatic changes in the protein under certain conditions. RNAP engaged with [lamda]Q escapes a [sigma]-mediated promoter proximal pause and overcomes an intrinsic terminator downstream of the pR' promoter. In addition, [lamda]Q alters RNAP dynamics, aiding faster elongation, fewer pauses, and resistance to both the intrinsic and [rho]-dependent termination. Although [lamda]Q-mediated antitermination was characterized with previous works as described above, the mechanism by which [lamda]Q exerts antitermination is still unclear. In order to uncover this mechanism, this study attempted to answer the fundamental question of where [lamda]Q interacts with RNAP. First, the two largest subunits of RNAP were systematically dissected to map a [lamda]Q binding region on RNAP. The results suggested a clustered region of three fragments of [beta] and [beta]' for [lamda]Q binding, and as small as 82 amino acids ([beta]600-681) within this region were identified to bind to [lamda]Q. Second, a potential [lamda]Q binding region of RNAP proposed by a previous study was evaluated in this study. Although the region is located in the surface domain of [beta]600- 681, mutational analyses targeting the region demonstrated little [lamda]Q binding. Third, twelve RNAP mutants that reduce [lamda]Q-mediated antitermination were identified, and they suggested four spatial regions of RNAP as critical for [lamda]Q antitermination. Finally, one of the RNAP mutants, [beta]K1073G, presented altered function of NusA, a transcription elongation factor, in [lamda]Q-mediated antitermination at the intrinsic terminator, providing evidence of cooperation between NusA and [lamda]Q antitermination.
Lambda II
Author: Roger W. Hendrix
Publisher:
ISBN:
Category : Science
Languages : en
Pages : 714
Book Description
Publisher:
ISBN:
Category : Science
Languages : en
Pages : 714
Book Description
Transcription Termination and Antitermination in Bacteriophage 82
Author: Jeffrey A. Goliger
Publisher:
ISBN:
Category : Bacteriophages
Languages : en
Pages : 488
Book Description
Publisher:
ISBN:
Category : Bacteriophages
Languages : en
Pages : 488
Book Description
PROTEINS INVOLVED IN PHAGE LAMBDA TRANSCRIPTION ANTITERMINATION (RIBOSOME, NUS GENES, RNA POLYMERASE).
Author: ALAN THOMAS SCHAUER
Publisher:
ISBN:
Category :
Languages : en
Pages : 103
Book Description
ribosome in the regulation of phage transcription.
Publisher:
ISBN:
Category :
Languages : en
Pages : 103
Book Description
ribosome in the regulation of phage transcription.
Regulation of Gene Expression in Escherichia coli
Author: E. C. C. Lin
Publisher: Springer Science & Business Media
ISBN: 1468486012
Category : Medical
Languages : en
Pages : 1010
Book Description
This up-to-date guide focuses on the understanding of key regulatory mechanisms governing gene expression in Escherichia coli. Studies of E. coli not only provide the first models of gene regulation, but research continues to yield different control mechanisms.
Publisher: Springer Science & Business Media
ISBN: 1468486012
Category : Medical
Languages : en
Pages : 1010
Book Description
This up-to-date guide focuses on the understanding of key regulatory mechanisms governing gene expression in Escherichia coli. Studies of E. coli not only provide the first models of gene regulation, but research continues to yield different control mechanisms.
Control of Late Transcription in Bacteriophage Lambda
Author: Donna L. Daniels
Publisher:
ISBN:
Category : Bacteriophage lambda
Languages : en
Pages : 466
Book Description
Publisher:
ISBN:
Category : Bacteriophage lambda
Languages : en
Pages : 466
Book Description
Lambda N Antitermination System: Functional Analysis of Phage Interactions with the Host NusA Protein
Author: Alan T. Schauer
Publisher:
ISBN:
Category :
Languages : en
Pages : 14
Book Description
Coliphage ambda gene expression is regulated temporally by systems of termination and antitermination of transcription. The lambda-encoded N protein (pN) acting with host factors (Nus) at sites (nut) located downstream from early promoters is the first of these systems to operate during phage development. We report observations on some of the components of this complex system that, in part, address the way in which these elements interact to render RNA polymerase termination-resistant. (1) The isolation of a conditionally lethal cold-sensitive nusA mutation demonstrates that NusA is essential for bacterial growth. (2) The effect on lambda growth in a host in which the Salmonella NusA protein is overproduced suggests that NusA is essential for N-mediated antitermination in phage lambda (3) A truncated NusA product, representing only the amino two-thirds of the native protein, is active for both bacterial growth and pN action, indicating that the carboxy end of the molecule may not be a functionally important region (4) lambdapN can function with the heterologous nut region from Salmonella typhimurium phage P22 when lambda pN is overproduced, demonstrating that lambda pN can function with the nut regions of other lambdoid phages. (5) A single base-pair change in the lambda nutR boxA sequence that was selected to permit a lambda derivative to utilize the Salmonella NusA protein restores lambda growth in the Escherichia colinusA1 host. (Reprints).
Publisher:
ISBN:
Category :
Languages : en
Pages : 14
Book Description
Coliphage ambda gene expression is regulated temporally by systems of termination and antitermination of transcription. The lambda-encoded N protein (pN) acting with host factors (Nus) at sites (nut) located downstream from early promoters is the first of these systems to operate during phage development. We report observations on some of the components of this complex system that, in part, address the way in which these elements interact to render RNA polymerase termination-resistant. (1) The isolation of a conditionally lethal cold-sensitive nusA mutation demonstrates that NusA is essential for bacterial growth. (2) The effect on lambda growth in a host in which the Salmonella NusA protein is overproduced suggests that NusA is essential for N-mediated antitermination in phage lambda (3) A truncated NusA product, representing only the amino two-thirds of the native protein, is active for both bacterial growth and pN action, indicating that the carboxy end of the molecule may not be a functionally important region (4) lambdapN can function with the heterologous nut region from Salmonella typhimurium phage P22 when lambda pN is overproduced, demonstrating that lambda pN can function with the nut regions of other lambdoid phages. (5) A single base-pair change in the lambda nutR boxA sequence that was selected to permit a lambda derivative to utilize the Salmonella NusA protein restores lambda growth in the Escherichia colinusA1 host. (Reprints).