Bacterial Serine/Threonine/Tyrosine Phosphoproteomics: A Current Status and Their Role in Diverse Biological Processes

Journal Title: INTERNATIONAL JOURNAL OF SCIENTIFIC STUDY - Year 2018, Vol 6, Issue 9

Abstract

Protein phosphorylation is the most common post-translational modification in proteins. The majority of amino acids modified in a protein are serine, threonine, and tyrosine. It is estimated that 30–60% of proteins in eukaryotes is phosphorylated and the role of these modifications is well studied. The protein phosphorylation is much less abundant in prokaryotes. The role of protein phosphorylation in prokaryotes is recently being realized. Identification of all the phosphoproteins present in a bacterial cell by high-resolution mass spectrometry and using gel-free protein digestion approaches has revolutionized the field. This review is mainly focused on the role of bacterial phosphoproteome and pathogenicity. A number of biochemical pathways such as glycolysis, translation, response to stress, sugar transport, and most importantly virulence are also regulated by protein phosphorylation.

Authors and Affiliations

Asha Mishra

Keywords

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  • EP ID EP483418
  • DOI -
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How To Cite

Asha Mishra (2018). Bacterial Serine/Threonine/Tyrosine Phosphoproteomics: A Current Status and Their Role in Diverse Biological Processes. INTERNATIONAL JOURNAL OF SCIENTIFIC STUDY, 6(9), 96-98. https://europub.co.uk/articles/-A-483418