A new target for CRP action at the malT promoter.

Menéndez, M. Carmen; Kolb, Annie; Buc, Henri

doi:10.1002/j.1460-2075.1987.tb02771.x

Cited by 71 publications

(50 citation statements)

References 32 publications

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“…For example, a deletion of Pc may allow an increased occupancy of RNA polymerase at hutUp to form closed or open complexes which may not result in the synthesis of run-off transcripts without further intervention of CAP-cAMP. In the case of malT, it was shown that RNA polymerase readily forms open complexes with the malT promoter but cannot make the transition to transcription elongation unless CAP-cAMP is present (27).…”

Section: Discussionmentioning

confidence: 99%

“…The CAP-cAMP complex specifically recognizes and binds a DNA sequence resembling the consensus AANTGTGAN6TCACANTT and can thereby activate or repress the transcription of a number of genes or operons (for reviews, see references 6, 8, 18, and 44). Considerable insight into the role of CAP-cAMP in regulating transcription has been gained from studies of promoters such as those in lac, gal, mal, and ara (7,8,15,22,23,27,44,47), from the crystal structure of CAP and its complex with DNA (48,56), and from mutagenic analysis of the protein (2,4,10,29,58). The generation of CAP mutants that are able to bind and bend DNA efficiently but are defective in transcription activation function provides evidence for a direct role of CAP-cAMP in activating transcription, which is thought to involve contacts between CAP and RNA polymerase (4,10,58).…”

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confidence: 99%

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Roles of catabolite activator protein sites centered at -81.5 and -41.5 in the activation of the Klebsiella aerogenes histidine utilization operon hutUH

1994

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The Klebsiella aerogenes hutUH operon is preceded by a promoter region, hut(P), that contains two divergent promoters (hutUp and Pc) which overlap and are alternately expressed. In the absence of the catabolite gene activator protein-cyclic AMP (CAP-cAMP) complex, Pc is predominantly expressed while hutUp is largely repressed. CAP-cAMP has the dual effect of repressing transcription from Pc while simultaneously activating transcription from hutUp. DNA deletion mutations in this region were used to identify DNA sequences required for transcription of these two promoters. We showed that inactivation of Pc by DNA deletion did not result in activation of hutUp in vitro or in vivo. In addition, Escherichia coli CAP mutants that are known to bind and bend DNA normally but are unable to activate various CAP-dependent promoters were also unable to activate hutUp in vivo. These results invalidate an indirect activation model by which CAP-mediated repression of Pc in itself would lead to activation of hutUp. Gel retardation assays with various deletion mutations of hut(P) and DNase I protection analyses revealed a high-affinity CAP binding site (CAP site 1) centered at -81.5 relative to the hutUp start of transcription and a second low-aflinity CAP site (CAP site 2) centered at about -41.5. CAP site 1 is essential for activation of hutUp. Although CAP site 2 by itself is unable to activate hutUp in vivo under catabolite-activating conditions, it appears to be required for maximal transcription activation. Our observation that the double CAP mutant crpH159L,K52N, which is known to activate transcription from a site centered at -41.5, does not activate hutUp suggests that the role of CAP-cAMP at the weaker CAP site may be different from that of other promoters containing a similarly positioned site. We propose that CAP directly stimulates the activity of RNA polymerase at hutUp and that this reaction is completely dependent on a naturally occurring CAP site centered at -81.5 and also involves a second CAP site centered at about -41.5 for maximal activation.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Roles of catabolite activator protein sites centered at -81.5 and -41.5 in the activation of the Klebsiella aerogenes histidine utilization operon hutUH

1994

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“…This review has focused on the lac system, but of great interest is whether what we have learned for lac can be generalized to other systems. Of particular concern are the obvious differences in the controlling element architecture (e.g., -61.5 for lac [3], -41.5 for gal [24]) and the apparent differences in the step in transcription initiation activated in different systems (RNA polymerase binding, closed-complex isomerization, or escape from the initiation to the elongation complex [10,14,15,17]). The evidence seems confusing.…”

Section: How Can the Differing Architectures Of Capmentioning

confidence: 99%

Catabolite gene activator protein activation of lac transcription

Reznikoff

1992

J Bacteriol

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“…Furthermore, mutations in 70 (4,48) and transcription activation (36) have been shown to affect the production of abortive products.…”

Section: Vol 188 2006 the Promoter And Antitermination 2229mentioning

confidence: 99%

Evidence that the Promoter Can Influence Assembly of Antitermination Complexes at Downstream RNA Sites

et al. 2006

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The N protein of phage acts with Escherichia coli Nus proteins at RNA sites, NUT, to modify RNA polymerase (RNAP) to a form that overrides transcription terminators. These interactions have been thought to be the primary determinants of the effectiveness of N-mediated antitermination. We present evidence that the associated promoter, in this case the early P R promoter, can influence N-mediated modification of RNAP even though modification occurs at a site (NUTR) located downstream of the intervening cro gene. As predicted by genetic analysis and confirmed by in vivo transcription studies, a combination of two mutations in P R , at positions ؊14 and ؊45 (yielding P R-GA ), reduces effectiveness of N modification, while an additional mutation at position ؊30 (yielding P R-GCA ) suppresses this effect. In vivo, the level of P R-GA -directed transcription was twice as great as the wild-type level, while transcription directed by P R-GCA was the same as that directed by the wild-type promoter. However, the rate of open complex formation at P R-GA in vitro was roughly one-third the rate for wild-type P R . We ascribe this apparent discrepancy to an effect of the mutations in P R-GCA on promoter clearance. Based on the in vivo experiments, one plausible explanation for our results is that increased transcription can lead to a failure to form active antitermination complexes with NUT RNA, which, in turn, causes failure to read through downstream termination sites. By blocking antitermination and thus expression of late functions, the effect of increased transcription through nut sites could be physiologically important in maintaining proper regulation of gene expression early in phage development.Expression of the delayed-early genes of coliphage is regulated by transcription termination and antitermination (19). Transcription initiating at the two early promoters P L and P R partially terminates at terminators t L1 and t R1 , respectively (Fig. 1A). Early transcription from P L results in production of N protein, which acts together with a number of host factors (Nus proteins) at NUT sites in nascent-early transcripts with RNA polymerase (RNAP) to form a transcription complex that is resistant to both intrinsic (Rho-independent) and Rhodependent terminators. Escherichia coli proteins that combine with N and NUT RNA to modify RNAP include NusA, NusB, ribosomal protein S10 (NusE), and NusG (10,23,40,43,55).Two classes of mutations in nus genes have been isolated. Class 1 mutations reduce effective N action, while class 2 mutations suppress the action of class 1 mutations by restoring the effectiveness of N in the presence of a class 1 mutation. For example, the failure of E. coli nusA1 or nusE71 mutants to support N action can be suppressed by class 2 mutations in either nusB or nusG (50,52). In addition to these class 2 nus mutations, a point mutation in rpoA, encoding the ␣ subunit of RNAP, suppresses the effects of nusA1 or nusE71 (47).With the exception of N, all phage-encoded factors required for lytic development ...

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A new target for CRP action at the malT promoter.

Cited by 71 publications

References 32 publications

Roles of catabolite activator protein sites centered at -81.5 and -41.5 in the activation of the Klebsiella aerogenes histidine utilization operon hutUH

Roles of catabolite activator protein sites centered at -81.5 and -41.5 in the activation of the Klebsiella aerogenes histidine utilization operon hutUH

Catabolite gene activator protein activation of lac transcription

Evidence that the Promoter Can Influence Assembly of Antitermination Complexes at Downstream RNA Sites

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