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Abstract: <br /> <br /> <br /> DnaJ is a chaperone which has function in facilitating folding, translocation, and degradation of protein. The aim of this research was to isolate gene encodes DnaJ from thermophilic bacteria, Bacillus sp. RP1 and to undertake in silico study of its...

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Bibliographic Details
Main Author: Kumaunang (NIM 205 03 025), Maureen
Format: Theses
Language:Indonesia
Online Access:https://digilib.itb.ac.id/gdl/view/8559
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Institution: Institut Teknologi Bandung
Language: Indonesia
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Summary:Abstract: <br /> <br /> <br /> DnaJ is a chaperone which has function in facilitating folding, translocation, and degradation of protein. The aim of this research was to isolate gene encodes DnaJ from thermophilic bacteria, Bacillus sp. RP1 and to undertake in silico study of its gene product. dnaf of Bacillus sp. RP1 was isolated by Polymerase Chain Reaction (PCR) method using DJF1 and DJR2 primers which were designed from nucleotide sequence of dnaJ B. stearothermophilus (Accession number Q45552). The size of the resulted DNA fragment was 1.1 kb. Analysis of 1053 bp from DNA fragment isolated by PCR showed that it has 97percent similarity with putative chaperone of Geobacillus kaustophilus (BA000043.1) and 86percent similarity with DnaK operon of B. stearothermophilus (X90709.1). dnaJ DNA fragment had been cloned into pGEM-T vector. Structure prediction of DnaJ Bacillus sp. RP1 showed that it has similar J-domain with that of DnaJ Escherichia coil but cys-rich domain is different.