Proteomic analysis of acidic chaperones, and stress proteins in extreme halophile Halobacterium NRC-1: a comparative proteomic approach to study heat shock response.

Proteome Science
H D Shukla

Abstract

Halobacterium sp. NRC-1 is an extremely halophilic archaeon and has adapted to optimal growth under conditions of extremely high salinity. Its proteome is highly acidic with a median pI of 4.9, a unique characteristic which helps the organism to adapt high saline environment. In the natural growth environment, Halobacterium NRC-1 encounters a number of stressful conditions including high temperature and intense solar radiation, oxidative and cold stress. Heat shock proteins and chaperones play indispensable roles in an organism's survival under many stress conditions. The aim of this study was to develop an improved method of 2-D gel electrophoresis with enhanced resolution of the acidic proteome, and to identify proteins with diverse cellular functions using in-gel digestion and LC-MS/MS and MALDI-TOF approach. A modified 2-D gel electrophoretic procedure, employing IPG strips in the range of pH 3-6, enabled improved separation of acidic proteins relative to previous techniques. Combining experimental data from 2-D gel electrophoresis with available genomic information, allowed the identification of at least 30 cellular proteins involved in many cellular functions: stress response and protein folding (CctB, PpiA, DpsA, and Msr...Continue Reading

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Nov 6, 2014·Life·Stefan LeukoBrendan P Burns
Jul 29, 2010·Molecular Systems Biology·Amardeep KaurNitin S Baliga
Dec 2, 2017·Environmental Microbiology·Lana J McMillanJulie A Maupin-Furlow
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Jan 22, 2013·Journal of Proteome Research·Fabio Aparecido CordeiroEmanuel Maltempi de Souza

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Methods Mentioned

BETA
protein folding
electrophoresis
protein assay

Software Mentioned

ImageMaster
MASCOT
ImageMaster 2D Elite
Image Master
SEQUEST
Excel

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