Post-translational Modification of Ribosomal Proteins

B. subtilis ribosomal proteins: structural homology and post-translational modifications.

Ribosomal proteins of the model gram-positive bacterium B. subtilis 168 were extensively characterized in a proteomic study. Mass spectra of the 52 proteins expected to be constitutive components of the 70S ribosome were recorded. Peptide MS/MS analysis with an average sequence coverage of 85% supported the identification of these proteins and facilitated the unambiguous assignment of post-tran...

Computational Prediction of Post-Translational Modification Sites in Proteins

The last several decades have witnessed rapid progresses in identification and functional analysis of post-translational modifications (PTMs) in proteins. Through temporal and spatial modification of proteins by covalent attachment of additional chemical groups and other small proteins, proteolytic cleavage or intein splicing, PTMs greatly expand the proteome diversity and play important roles ...

Post-translational modification of PII signal transduction proteins

The PII proteins constitute one of the most widely distributed families of signal transduction proteins in nature. They are pivotal players in the control of nitrogen metabolism in bacteria and archaea, and are also found in the plastids of plants. Quite remarkably PII proteins control the activities of a diverse range of enzymes, transcription factors and membrane transport proteins, and in al...

Post-translational modification and folding of secreted proteins.

The production of a functional protein does not end with the termination of the growing polypeptide chain. This, while clearly true of all proteins, is particularly obvious in the case of secretory proteins. While all proteins must fold to a functional conformation, and many must assemble into some supramolecular structure, secretory proteins must also make their way across membranes and throug...

Post-translational modification of exogenous proteins in Xenopus laevis oocytes.