ABSTRACT
Proteins containing the NIF3 domain are highly conserved and are found in bacteria, eukaryotes, and archaea. YbgI is an Escherichia coli protein whose gene is conserved among bacteria. The structure of YbgI is known; however, the function of this protein in cells remains obscure. Our studies of E. coli cells with deleted ybgI gene suggest that YbgI is involved in formation of the bacterial cell wall.
Subject(s)
Escherichia coli Proteins/metabolism , Escherichia coli/metabolism , Cell Wall/metabolism , Conserved Sequence , Escherichia coli/cytology , Escherichia coli Proteins/chemistry , Escherichia coli Proteins/genetics , Gene Deletion , Protein DomainsABSTRACT
In this work we describe methodology for studying the role of bacterial ribosome modification in the regulation of gene expression. Ribosomal components modification influences translation efficiencies of certain mRNAs. Proteome analysis allows us to identify cellular protein composition change caused by ribosome modification gene knockout. Particular stage of gene expression responsible for certain protein concentration change could be found using reporter constructs. After identification of mRNA species, whose translation is influenced by ribosome modification we can determine exact mRNA region responsible for the observed changes. The developed methodology can be applied for studying other translational control mechanisms.
Subject(s)
Bacterial Proteins/biosynthesis , Escherichia coli/metabolism , Methyltransferases/metabolism , Proteome/analysis , RNA, Bacterial/metabolism , RNA, Ribosomal/metabolism , Ribosomes/metabolism , Bacterial Proteins/genetics , Electrophoresis, Gel, Two-Dimensional , Escherichia coli/genetics , Gene Expression Regulation, Bacterial , Genes, Reporter , Immunoblotting , Lac Operon , Luciferases/genetics , Methyltransferases/genetics , RNA Processing, Post-Transcriptional , RNA, Messenger/biosynthesis , RNA, Messenger/genetics , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , beta-Galactosidase/biosynthesis , beta-Galactosidase/geneticsABSTRACT
Рnumber 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.
