Structure of two divergent promoters located in front of the gene encoding pullulanase in Klebsiella pneumoniae and positively regulated by the malT product
Journal of BacteriologyPublished 1 November 1985Open access
C Chapon, Olivier Raibaud
Citations58
SJR quartileQ2
SJR score1.09
SNIP0.85
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TL;DR
Characterization of the region 59 to pulA and of the beginning of the gene described herein demonstrate that pullulanase is probably a lipoprotein and an additional malT-controlled promoter lies adjacent to the pulA promoter and is oriented in the opposite direction.
Abstract
Pullulanase is an extracellular starch-debranching enzyme produced by Klebsiella pneumoniae. When its structural gene, pulA, is introduced into Escherichia coli, it is controlled by malT, the positive regulator gene of the maltose regulon. Characterization of the region 5' to pulA and of the beginning of the gene described herein demonstrate that (i) pullulanase is probably a lipoprotein; (ii) an additional malT-controlled promoter (the malX promoter) lies adjacent to the pulA promoter and is oriented in the opposite direction; (iii) in common with the three previously described malT-controlled promoters, the pulA and malX promoters have a conserved hexanucleotide (consensus sequence, 5'-GGATGGA) 35 base pairs upstream from the transcription initiation site; and (iv) upstream from this conserved hexanucleotide the pulA and malX promoters differ from the other mal promoters in that they lack any detectable binding site for the cyclic AMP-binding protein.
Keywords
Biochemistry, Genetics and Molecular BiologyEnvironmental Science
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