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    Molecular diversity of RelA enzyme in marine bacteria- A bioinformatics analysis

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    Biodeiversity_Environ_Sustain_2008_199.pdf (41.80Kb)
    Date
    2008
    Author
    Nath, A.I.V.
    Tresa, R.A.T.
    Alornekar, A.
    Varghese, N.S.
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    Abstract
    The RelA (relaxed) protein is a crucial protein related to unculturability in bacteria. In response to nutrient scarcity, most of the marine bacteria are known to enter a viable but non-culturable (VBNC) state, but remain intact and retain viability. It has been shown that VBNC cells remain potentially pathogenic. The RelA protein is a ribosome-associated Guanosine-3'-diphosphate-5'-diphosphate (ppGpp) synthetase that is activated by amino acid deprivation. It belongs to the spoT/relA family of proteins. The RelA enzyme is present in different marine bacteria. Since the VBNC state is generally implicated in pathogenesis and the outbreak of diseases, the molecular study of RelA is important. Hence, the present study analyzes the data of the RelA enzyme from 4 different marine bacterial genera expressing a VBNC response. The protein sequences of some species like Escherichia coli, Vibrio vulnificus, Streptomyces coelicolor and Campylobacter jejuni have been accessed from a NCBI database for comparison and analysis. Multiple sequence alignment using Clustal W2 showed a high degree of conservation amino acid residues between 300-360 and 430-580 in the protein chain. The paper discusses the molecular characterization of active sites of the RelA enzyme which would be useful in developing potential inhibitors for the enzyme activity. Such an attempt would help evolve a method for improving the culturing of bacteria undergoing the VBNC state
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    http://drs.nio.org/drs/handle/2264/1474
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