1987
DOI: 10.1093/nar/15.5.2343
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Analysis of E.Coli Pormoter sequences

Abstract: We have compiled and analyzed 263 promoters with known transcriptional start points for E. coli genes. Promoter elements (-35 hexamer, -10 hexamer, and spacing between these regions) were aligned by a program which selects the arrangement consistent with the start point and statistically most homologous to a reference list of promoters. The initial reference list was that of Hawley and McClure (Nucl. Acids Res. 11, 2237-2255, 1983). Alignment of the complete list was used for reference until successive analyse… Show more

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Cited by 1,020 publications
(813 citation statements)
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References 130 publications
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“…2), which matches the proposed -35 and -10 promoter regions deduced from the DNA sequence. It also matches a typical procaryotic start point of transcription, whose consensus is pyrimidine-purine-pyrimidine, starting with the purine CGT (19). Primer extension confirmed the T2 nuclease results (data not shown).…”
Section: Resultssupporting
confidence: 71%
“…2), which matches the proposed -35 and -10 promoter regions deduced from the DNA sequence. It also matches a typical procaryotic start point of transcription, whose consensus is pyrimidine-purine-pyrimidine, starting with the purine CGT (19). Primer extension confirmed the T2 nuclease results (data not shown).…”
Section: Resultssupporting
confidence: 71%
“…The resulting Preliminary pClone -35 Consensus is shown in Figure 5B. It differs considerably from the published -35 consensus shown in Figure 5A, which was derived from 263 E. coli promoters (Harley & Reynolds, 1987). Specifically, the first, second, third, and fifth bases differ between the two consensus sequences.…”
Section: Consensus Sequence Determinationmentioning
confidence: 87%
“…The restriction sites were first placed using the restriction digests given in Table 13, and then ordened in detail with the help of restriction fragments electrophoresed and sized on acrylamide gels (see Table 14 3030, 1980, 1980, 53O 3230, e640, 122A, 35O 3570,3360,480 2080, 1610, 1250, 70O, 640, 340, 2gO, 170, I Tables ls and l4 (TriggsRaine and Loewen, 1987). was determined from the restriction enzyme digests given in Table l7 and the restriction rnap is shown in Figure ll. pBTS was transforn¡ed into the catalase deficient mutant UH53, but it was unable to conplement the catalase nrutation (see Table l6 (Harley and Reynolds, 1987), lVeaKly conserved bases (occurrng in 377, or less of l, coÌi pronwters, [Harley and Reynolds, 19871) are also shown in Figure 24. Two The group blocking the N-terminus of bovine I iver catalase has not been identified even with the help of x-ray crystal lography and positive and negative ion nnss spectrometry (Schroeder et al,l9B2a (Loewen et al, 1985b) and 78 00o (cìaiþorne and Fridovich,1gr9) est irnated by SDS-PAGE.…”
Section: Catalase and Penoxidase Visual Ization On Polyacrylanide Gelsmentioning
confidence: 99%