1887

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Volume 161, Issue 9

is subject to phosphotransferase system-dependent regulation in Free

Abstract

The Gram-positive co-metabolizes most carbon sources such as the phosphotransferase system (PTS) sugar glucose and the non-PTS sugar maltose. Maltose is taken up via the ABC-transporter MusEFGKI, and is further metabolized to glucose phosphate by amylomaltase MalQ, maltodextrin phosphorylase MalP, glucokinase Glk and phosophoglucomutase Pgm. Surprisingly, growth of strains lacking the general PTS components EI or HPr was strongly impaired on the non-PTS sugar maltose. Complementation experiments showed that a functional PTS phosphorelay is required for optimal growth of on maltose, implying its involvement in the control of maltose metabolism and/or uptake. To identify the target of this PTS-dependent control, transport measurements with C-labelled maltose, Northern blot analyses and enzyme assays were performed. The activities of the maltose transporter and enzymes MalQ, Pgm and GlK were not decreased in PTS-deficient strains, which was corroborated by comparable transcript amounts of , and , as well as of , in Δ and WT. By contrast, MalP activity was significantly reduced and only residual amounts of transcripts were detected in Δ when compared to WT. Promoter activity assays with the promoter in Δ and WT confirmed that transcription is reduced in the PTS-deficient strain. Taken together, we show here for what is to the best of our knowledge the first time a regulatory function of the PTS in and identify transcription as its target.

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2015-09-01
2024-04-25
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Transcription of malP is subject to phosphotransferase system-dependent regulation in Corynebacterium glutamicum
Microbiology 161, 1830 (2015); https://doi.org/10.1099/mic.0.000134
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