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dc.contributorYeshvekar, Richa K.en_US
dc.contributorSharma, Kiranen_US
dc.contributorVadez, Vincenten_US
dc.contributorReddy, Malireddy K.en_US
dc.contributorReddy, P. Sudhakaren_US
dc.creatorNitnavare, Rahul B.en_US
dc.date.accessioned2017-04-01T20:46:37Z
dc.date.available2017-04-01T20:46:37Z
dc.identifierhttp://oar.icrisat.org/id/eprint/9535en_US
dc.identifierhttps://mel.cgiar.org/reporting/download/hash/LWcMcaIaen_US
dc.identifier.citationRahul B. Nitnavare, Richa K. Yeshvekar, Kiran Sharma, Vincent Vadez, Malireddy K. Reddy, P. Sudhakar Reddy. (20/5/2016). Molecular cloning, characterization and expression analysis of a heat shock protein 10 (Hsp10) from Pennisetum glaucum (L. ), a C4 cereal plant from the semi-arid tropics. Molecular Biology Reports, 43 (8), pp. 861-870.en_US
dc.identifier.urihttps://hdl.handle.net/20.500.11766/6559
dc.description.abstractHeat shock proteins (Hsp10) belong to the ubiquitous family of heat-shock molecular chaperones found in the organelles of both prokaryotes and eukaryotes. Chaperonins assist the folding of nascent and stressdestabilized proteins. A cDNA clone encoding a 10 kDa Hsp was isolated from pearl millet, Pennisetum glaucum (L.) by screening a heat stress cDNA library. The fulllength PgHsp10 cDNA consisted of 297 bp open reading frame (ORF) encoding a 98 amino acid polypeptide with a predicted molecular mass of 10.61 kDa and an estimated isoelectric point (pI) of 7.95. PgHsp10 shares 70–98 % sequence identity with other plant homologs. Phylogenetic analysis revealed that PgHsp10 is evolutionarily close to the maize Hsp10 homolog. The predicted 3D model confirmed a conserved eight-stranded ß-barrel with active site between the ß-barrel comprising of eight-strands, with conserved domain VLLPEYGG sandwiched between two ß-sheets. The gene consisted of 3 exons and 2 introns, while the position and phasing of these introns were conserved similar to other plant Hsp10 family genes. In silico analysis of the promoter region of PgHsp10 presented several distinct set of cis-elements and transcription factor binding sites. Quantitative RT-PCR analysis showed that PgHsp10 gene was differentially expressed in response to abiotic stresses with the highest level of expression under heat stress conditions. Results of this study provide useful information regarding the role of chaperonins in stress regulation and generated leads for further elucidation of their function in plant stress toleranceen_US
dc.formatPDFen_US
dc.languageenen_US
dc.publisherSpringer Verlag (Germany)en_US
dc.rightsCC-BY-NC-4.0en_US
dc.sourceMolecular Biology Reports;43,(2016) Pagination 861,870en_US
dc.subjectheat stress cdna libraryen_US
dc.subjectchaperoninen_US
dc.subjectPearl milleten_US
dc.titleMolecular cloning, characterization and expression analysis of a heat shock protein 10 (Hsp10) from Pennisetum glaucum (L.), a C4 cereal plant from the semi-arid tropicsen_US
dc.typeJournal Articleen_US
dcterms.available2016-05-20en_US
dcterms.extent861-870en_US
cg.creator.idVadez, Vincent: 0000-0003-2014-0281en_US
cg.subject.agrovocagricultureen_US
cg.subject.agrovocpennisetum glaucumen_US
cg.subject.agrovocabaen_US
cg.contributor.centerInternational Crops Research Institute for the Semi-Arid Tropics - ICRISATen_US
cg.contributor.centerInternational Centre for Genetic Engineering and Biotechnologyen_US
cg.contributor.crpCRP on Dryland Cereals - DCen_US
cg.contributor.funderNot Applicableen_US
cg.date.embargo-end-date2017-05-20en_US
cg.coverage.regionSouthern Asiaen_US
cg.coverage.countryINen_US
cg.contactp.sudhakarreddy@cgiar.orgen_US
cg.identifier.doihttps://dx.doi.org/10.1007/s11033-016-4012-0en_US
cg.isijournalISI journalen_US
dc.identifier.statusLimited accessen_US
mel.impact-factor1.698en_US
cg.issn0301-4851en_US
cg.journalMolecular Biology Reportsen_US
cg.issue8en_US
cg.volume43en_US


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