کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
9121631 1159193 2005 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Dual phosphorylation of Mycoplasma pneumoniae HPr by Enzyme I and HPr kinase suggests an extended phosphoryl group susceptibility of HPr
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی ژنتیک
پیش نمایش صفحه اول مقاله
Dual phosphorylation of Mycoplasma pneumoniae HPr by Enzyme I and HPr kinase suggests an extended phosphoryl group susceptibility of HPr
چکیده انگلیسی
In Gram-positive bacteria, the HPr protein of the phosphoenolpyruvate:sugar phosphotransferase system can be phosphorylated at two distinct sites, His-15 and Ser-46. While the former phosphorylation is implicated in phosphoryl transfer to the incoming sugars, the latter serves regulatory purposes. In Bacillus subtilis, the two phosphorylation events are mutually exclusive. In contrast, doubly phosphorylated HPr is present in cell extracts of Mycoplasma pneumoniae. In this work, we studied the ability of the two single phosphorylated HPr species to accept a second phosphoryl group. Indeed, both Enzyme I and the HPr kinase/phosphorylase from M. pneumoniae are able to use phosphorylated HPr as a substrate. The formation of doubly phosphorylated HPr is substantially slower as compared to the phosphorylation of free HPr. However, the rate of formation of doubly phosphorylated HPr is sufficient to account for the amount of HPr(His∼P)(Ser-P) detected in M. pneumoniae cells.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEMS Microbiology Letters - Volume 247, Issue 2, 15 June 2005, Pages 193-198
نویسندگان
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