Disease relevance of malT

• Comparison of the malA regions of Escherichia coli and Klebsiella pneumoniae [1].
• Using the mini-Mu-duction technique, we cloned the malA regions from Escherichia coli K-12 and Klebsiella pneumoniae [1].
• A series of plaque-forming lambda h80 transducing phages carrying various portions of the malA region were isolated [2].
• Among the markers expressed in Proteus hybrids with the E. coli malA region was the receptor site for coliphage lambda [3].
• Similarly, the prophage site and malA were cotransduced by T4GT7 but not by P1 [4].

High impact information on malT

• Secretion genes located 5' to pulA were transcribed in the opposite orientation to pulA under the control of the previously identified, malT-regulated malX promoter [5].
• These mutants are also altered in positive control at the lac and malT promoters, where CAP binds to sites further upstream from the transcription start site [6].
• Expression of the Escherichia coli maltose regulon is controlled by MalT, a transcriptional activator (Mr = 102,288) encoded by the malT gene [7].
• The mlc gene encodes a transcriptional regulator that has been shown to affect the expression of manXYZ and malT. ptsG mRNA levels are lower in the mlc strain grown on glucose than in the same strain grown on glycerol [8].
• The malA region of Escherichia coli contains one of the three maltose operons, namely malPQ, and the positive regulatory gene, malT [9].

Chemical compound and disease context of malT

• The pores of the C. crescentus porins are slightly larger than those of E. coli K-12, since maltotetraose supported growth of the C. crescentus malA mutant but failed to support growth of the E. coli lamB mutant [10].
• Permeation of maltose and maltotriose through the outer membrane of the C. crescentus malA mutant was slower than permeation through the outer membrane of an E. coli lamB mutant, which suggests a low porin activity in C. crescentus [10].

Biological context of malT

• A DNA sequence containing the control sites for gene malT and for the malPQ operon [11].
• The order of 802 base pairs was established in a DNA segment containing the promoter for malPQ which is one of the three maltose operons, and the promoter for malT, the positive regulator gene of the maltose regulon [11].
• By deleting in vitro the 3'-end of the gene or constructing malT-lacZ gene fusions, it was found that the integrity of the C-terminus of MalT is indispensable for the activity of the protein [12].
• However this requirement is lost when the expression of malT, positive regulator gene of the maltose regulon, is rendered independent of CAP by a mutation in the malT promoter [13].
• A restriction map of the HindIII-EcoRI fragment was established, and it was correlated with the genetic map of the malA region (i) by mapping deletions which had been generated in vitro on the plasmid and (ii) by locating on the restriction map a DNA insertion of known genetic position [2].

Associations of malT with chemical compounds

• The malA mutant was unable to grow on maltodextrins larger than maltotetraose [10].

Other interactions of malT

• Reconstitution of maltose transport in malB and malA mutants of Escherichia coli [14].

References