Posttranslational Modifications of Ribosomal Proteins in Escherichia coli

نویسندگان

  • M.V. Nesterchuk
  • P.V. Sergiev
  • O.A. Dontsova
چکیده

А number of ribosomal proteins inEscherichia coliundergo posttranslational modifications. Six ribosomal proteins are methylated (S11, L3, L11, L7/L12, L16, and L33), three proteins are acetylated (S5, S18, and L7), and protein S12 is methylthiolated. Extra amino acid residues are added to protein S6. С-terminal amino acid residues are partially removed from protein L31. The functional significance of these modifications has remained unclear. These modifications are not vital to the cells, and it is likely that they have regulatory functions. This paper reviews all the known posttranslational modifications of ribosomal proteins inEscherichia coli. Certain enzymes responsible for the modifications and mechanisms of enzymatic reactions are also discussed.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

High Level Expression of Recombinant Ribosomal Protein (L7/L12) from Brucella abortus and Its Reaction with Infected Human Sera

Brucellosis, caused by Brucella spp., is an important zoonotic disease that causes abortion and infertility in cattle and undulant fever in humans. Various studies have examined cell-free native and recombinant proteins as candidate protective antigens in animal models. Among Brucella immunogenes, antigen based on ribosomal preparation has been widely investigated. In this study, the immunogeni...

متن کامل

Enterotoxigenic Escherichia coli infection induces tight junction proteins expression in mice

Enterotoxigenic Escherichia coli (ETEC) causes diarrhea in travelers, young children and piglets, but the precise pathogenesis of ETEC induced diarrhea is not fully known. Recent investigations have shown that tight junction (TJ) proteins and aquaporin 3 (AQP 3) are contributing factors in bacterial diarrhea. In this study, using immunoblotting and immunohistochemistry analyses, we found that E...

متن کامل

Correlating the chemical modification of Escherichia coli ribosomal proteins with crystal structure data.

Various chemical modifications have been applied to study protein structures. In this paper, amidination of E. coli ribosomal proteins was investigated to profile the structure of this large protein/RNA complex. The extent of ribosomal protein amidination was correlated with the solvent accessibility of amine groups in E. coli ribosome crystal structures. The modification of many residues was c...

متن کامل

Identification by affinity chromatography of the rat liver ribosomal proteins that bind to Escherichia coli 5 S ribosomal ribonucleic acid.

The eukaryotic and prokaryotic ribosomal proteins that bind to Escherichia coli 5 S rRNA were identified by affinity chromatography. The E. coli ribosomal proteins that associated with the nucleic acid were L5, L18, and L25 confirming earlier findings using the same and different procedures. The rat liver ribosomal proteins that associated with E. coli 5 S rRNA were L6, L7, L19, L35a, and S9; s...

متن کامل

Stability of Recombinant Proteins in Escherichia coli: The Effect of Co-Expression of Five Different Chaperone Sets

Chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. Over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell. On the basis of this hypothesis, five different plasmids with 5 different combinations of 6 chaperones molecule, transformed into Escherichia coli along with human basic Fibroblast Grow...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 3  شماره 

صفحات  -

تاریخ انتشار 2011