کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1937852 | 1050727 | 2007 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Three UDP-hexose 4-epimerases with overlapping substrate specificity coexist in E. coli O86:B7
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The O-antigen gene cluster of Escherichia coli O86:B7 was sequenced previously in our lab. One UDP-hexose 4-epimerase gene (named gne2 in this paper) was found and later characterized to be able to catalyze the interconversion between UDP-GlcNAc/GalNAc and UDP-Glc/Gal with almost equal efficiency. However, sequencing of the flanking gene region upstream of the traditional O-antigen gene cluster revealed an open reading frame (gne1), sharing 100% identity with Gne from E. coli O55, previously identified as UDP-GlcNAc 4-epimerase. Furthermore, we also located the traditional galE gene in the gal operon of O86:B7, which can catalyze the interconversion of UDP-Glc to UDP-Gal. Thus, for the first time, three UDP-hexose 4-epimerases with overlapping substrate specificity were found to coexist in one bacterium. Deletion of gne1 and gne2 in O86:B7 produced two different LPS phenotypes: the gne1 mutant exhibited rough LPS, while the gne2 mutant showed semi-rough LPS phenotype. These findings provide new clues for understanding the mechanism of O-antigen biosynthesis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 356, Issue 3, 11 May 2007, Pages 604-609
Journal: Biochemical and Biophysical Research Communications - Volume 356, Issue 3, 11 May 2007, Pages 604-609
نویسندگان
Hongjie Guo, Wen Yi, Lei Li, Peng George Wang,