scholarly journals The cAMP receptor protein of Trypanosoma cruzi.

1983 ◽  
Vol 258 (11) ◽  
pp. 6979-6983 ◽  
Author(s):  
R Rangel-Aldao ◽  
G Tovar ◽  
M Ledezma de Ruiz
Keyword(s):  
Trypanosoma Cruzi ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Camp Receptor

scholarly journals Interactions between the Escherichia coli cAMP receptor protein and the C-terminal domain of the α subunit of RNA polymerase at Class I promoters

1999 ◽  
Vol 337 (3) ◽  
pp. 415-423 ◽  
Author(s):  
Emma C. LAW ◽  
Nigel J. SAVERY ◽  
Stephen J. W. BUSBY
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Transcription Initiation ◽  
Class I ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Α Subunit ◽  
Terminal Domain ◽  
Up Elements ◽  
Camp Receptor

The Escherichia coli cAMP receptor protein (CRP) is a factor that activates transcription at over 100 target promoters. At Class I CRP-dependent promoters, CRP binds immediately upstream of RNA polymerase and activates transcription by making direct contacts with the C-terminal domain of the RNA polymerase α subunit (αCTD). Since αCTD is also known to interact with DNA sequence elements (known as UP elements), we have constructed a series of semi-synthetic Class I CRP-dependent promoters, carrying both a consensus DNA-binding site for CRP and a UP element at different positions. We previously showed that, at these promoters, the CRP–αCTD interaction and the CRP–UP element interaction contribute independently and additively to transcription initiation. In this study, we show that the two halves of the UP element can function independently, and that, in the presence of the UP element, the best location for the DNA site for CRP is position -69.5. This suggests that, at Class I CRP-dependent promoters where the DNA site for CRP is located at position -61.5, the two αCTDs of RNA polymerase are not optimally positioned. Two experiments to test this hypothesis are presented.

scholarly journals Identification and Characterization of a Novel cAMP Receptor Protein in the CyanobacteriumSynechocystissp. PCC 6803

2000 ◽  
Vol 275 (9) ◽  
pp. 6241-6245 ◽  
Author(s):  
Hidehisa Yoshimura ◽  
Toru Hisabori ◽  
Shuichi Yanagisawa ◽  
Masayuki Ohmori
Keyword(s):  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Camp Receptor ◽  
Identification And Characterization ◽  
Pcc 6803

scholarly journals Regulation of the expression of whiB1 in Mycobacterium tuberculosis: role of cAMP receptor protein

Microbiology ◽  
2006 ◽  
Vol 152 (9) ◽  
pp. 2749-2756 ◽  
Author(s):  
Nisheeth Agarwal ◽  
Tirumalai R. Raghunand ◽  
William R. Bishai
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Binding Site ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Mobility Shift ◽  
Camp Analogue ◽  
Camp Receptor ◽  
Fusion Analysis ◽  
Electrophoretic Mobility Shift Assays

The wbl (whiB-like) genes encode putative transcription factors unique to actinomycetes. This study characterized the promoter element of one of the seven wbl genes of Mycobacterium tuberculosis, whiB1 (Rv3219c). The results reveal that whiB1 is transcribed by a class I-type cAMP receptor protein (CRP)-dependent promoter, harbouring a CRP-binding site positioned at −58.5 with respect to its transcription start point. In vivo promoter activity analysis and electrophoretic mobility shift assays suggest that the expression of whiB1 is indeed regulated by cAMP-dependent binding of CRPM (encoded by the M. tuberculosis gene Rv3676) to the whiB1 5′ untranslated region (5′UTR). β-Galactosidase gene fusion analysis revealed induction of the whiB1 promoter in M. tuberculosis on addition of exogenous dibutyric cAMP (a diffusible cAMP analogue) only when an intact CRP-binding site was present. These results indicate that M. tuberculosis whiB1 transcription is regulated in part by cAMP levels via direct binding of cAMP-activated CRPM to a consensus CRP-binding site in the whiB1 5′UTR.

scholarly journals Thermodynamics of Cyclic Nucleotide Binding to the cAMP Receptor Protein and Its T127L Mutant

1995 ◽  
Vol 270 (37) ◽  
pp. 21679-21683 ◽  
Author(s):  
Inna Gorshkova ◽  
Julie L. Moore ◽  
Keith H. McKenney ◽  
Frederick P. Schwarz
Keyword(s):  
Cyclic Nucleotide ◽  
Nucleotide Binding ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Cyclic Nucleotide Binding ◽  
Camp Receptor

scholarly journals Repression of VvpM Protease Expression by Quorum Sensing and the cAMP-cAMP Receptor Protein Complex inVibrio vulnificus

2018 ◽  
Vol 200 (7) ◽  
Author(s):  
Jeong-A Kim ◽  
Mi-Ae Lee ◽  
You-Chul Jung ◽  
Bo-Ram Jang ◽  
Kyu-Ho Lee
Keyword(s):  
Transcription Factors ◽  
Stationary Phase ◽  
Cell Density ◽  
Transcription Initiation ◽  
Vibrio Vulnificus ◽  
The Other ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Content Type ◽  
Camp Receptor

ABSTRACTSepticemia-causingVibrio vulnificusproduces at least three exoproteases, VvpE, VvpS, and VvpM, all of which participate in interactions with human cells. Expression of VvpE and VvpS is induced in the stationary phase by multiple transcription factors, including sigma factor S, SmcR, and the cAMP-cAMP receptor protein (cAMP-CRP) complex. Distinct roles of VvpM, such as induction of apoptosis, lead us to hypothesize VvpM expression is different from that of the other exoproteases. Its transcription, which was found to be independent of sigma S, is induced at the early exponential phase and then becomes negligible upon entry into the stationary phase. SmcR and CRP were studied regarding the control ofvvpMexpression. Transcription ofvvpMwas repressed by SmcR and cAMP-CRP complex individually, which specifically bound to the regions −2 to +20 and +6 to +27, respectively, relative to thevvpMtranscription initiation site. Derepression ofvvpMgene expression was 10- to 40-fold greater in ansmcR crpdouble mutant than in single-gene mutants. Therefore, these results show that the expression ofV. vulnificusexoproteases is differentially regulated, and in this way, distinct proteases can engage in specific interactions with a host.IMPORTANCEAn opportunistic human pathogen,Vibrio vulnificusproduces multiple extracellular proteases that are involved in diverse interactions with a host. The total exoproteolytic activity is detected mainly in the supernatants of the high-cell-density cultures. However, some proteolytic activity derived from a metalloprotease, VvpM, was present in the supernatants of the low-cell-density cultures sampled at the early growth period. In this study, we present the regulatory mechanism for VvpM expression via repression by at least two transcription factors. This type of transcriptional regulation is the exact opposite of those for expression of the otherV. vulnificusexoproteases. Differential regulation of each exoprotease's production then facilitates the pathogen's participation in the distinct interactions with a host.

Sign in / Sign up

Export Citation Format

Share Document