کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1928073 1050309 2015 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Presence of an amino acid residue at position 619 required for the function of YidC in Rhodobacter sphaeroides
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Presence of an amino acid residue at position 619 required for the function of YidC in Rhodobacter sphaeroides
چکیده انگلیسی


• Rhodobacter sphaeroides YidC could restore the growth the YidC deletion mutation FTL10.
• The deletion of the last 5 amino acid residues abolished the function of the Rs_YidC.
• Presence of an amino acid residue at position 619 is required for the Rs_YidC activity.

YidC, the bacterial homologous protein of Oxa1 and Alb3, could insert membrane proteins into the membrane. Rhodobacter sphaeroides is a kind of photobacteria with abundant intracytoplasmic membranes. In this study, the functions of R. sphaeroides YidC and its C-terminus were investigated in the Escherichia coli YidC gene depletion strain FTL10. The results showed that RS_YidC could complement the growth of the strain FTL10, but the RS_YidC last 5 residues (619–623, KKRKP) deletion mutant could not. Interestingly, the site-directed RS_YidC mutants of any one or all of these 5 residues were still active. The deletion mutant of the last 4 residues and even the last 4 residues deletion mutant with substitution of the Ala or Glu for Lys619 still had sufficient activity to complement the growth of the strain FTL10. These results indicated that the length of the C-terminus of Rs_YidC is more important for its function than the amino acid composition or the charges of it, and the presence of an amino acid residue at position 619 is required for Rs_YidC function in E. coli. Our result also suggests that Rs_YidC may function differently as compared to its homologs.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 466, Issue 2, 16 October 2015, Pages 267–271
نویسندگان
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