<mets:mets OBJID="eprint_10134" LABEL="Eprints Item" xsi:schemaLocation="http://www.loc.gov/METS/ http://www.loc.gov/standards/mets/mets.xsd http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-3.xsd" xmlns:mets="http://www.loc.gov/METS/" xmlns:mods="http://www.loc.gov/mods/v3" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"><mets:metsHdr CREATEDATE="2023-07-05T01:14:26Z"><mets:agent ROLE="CUSTODIAN" TYPE="ORGANIZATION"><mets:name>OAR@ICRISAT</mets:name></mets:agent></mets:metsHdr><mets:dmdSec ID="DMD_eprint_10134_mods"><mets:mdWrap MDTYPE="MODS"><mets:xmlData><mods:titleInfo><mods:title>Heat responsive proteome changes reveal molecular mechanisms underlying heat tolerance in chickpea</mods:title></mods:titleInfo><mods:name type="personal"><mods:namePart type="given">P</mods:namePart><mods:namePart type="family">Santisree</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">P</mods:namePart><mods:namePart type="family">Bhatnagar-Mathur</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">K K</mods:namePart><mods:namePart type="family">Sharma</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:abstract>Understanding the molecular differences in plant genotypes contrasting for heat sensitivity can provide useful insights into the mechanisms that confer heat tolerance in plants. This study focuses on comparative physiological and proteomic analyses of heat-sensitive (ICC16374) and heat-tolerant (JG14) genotypes of chickpea (Cicer arietinum L.) under heat stress impositions at anthesis. Heat stress reduced leaf water content, chlorophyll content and membrane integrity with a greater impact on the sensitive genotype compared to the tolerant one that had higher total antioxidant capacity and osmolyte accumulation, and consequently less oxidative damage. This study identified a set of 482 heat-responsive proteins in the tolerant genotype using comparative gel-free proteomics. Besides heat shock proteins, proteins such as acetyl-CoA carboxylase, pyrroline-5-carboxylate synthase (P5CS), ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), phenylalanine ammonia-lyase (PAL) 2, ATP synthase, glycosyltransferase, sucrose synthase and late embryogenesis abundant (LEA) proteins were strongly associated with heat tolerance in chickpea. Several crucial proteins were induced by heat exclusively in the heat-tolerant genotype. Comparative proteome profiling and pathway analysis revealed mitigating strategies including, accumulation of osmoprotectants, protected membrane transport, ribosome and secondary metabolite synthesis, activation of antioxidant and defense compounds, amino acid biosynthesis, and hormonal modulation that might play key roles in chickpea heat tolerance. This study potentially contributes to improved stress resilience by advancing our understanding on the mechanisms of heat tolerance in chickpea.</mods:abstract><mods:classification authority="lcc">Molecular Biology</mods:classification><mods:classification authority="lcc">Chickpea</mods:classification><mods:classification authority="lcc">Genetics and Genomics</mods:classification><mods:classification authority="lcc">Climate Change</mods:classification><mods:originInfo><mods:dateIssued encoding="iso8061">2017-09</mods:dateIssued></mods:originInfo><mods:originInfo><mods:publisher>Elsevier</mods:publisher></mods:originInfo><mods:genre>Article</mods:genre></mets:xmlData></mets:mdWrap></mets:dmdSec><mets:amdSec ID="TMD_eprint_10134"><mets:rightsMD ID="rights_eprint_10134_mods"><mets:mdWrap MDTYPE="MODS"><mets:xmlData><mods:useAndReproduction>
<p xmlns="http://www.w3.org/1999/xhtml"><strong>For work being deposited by its own author:</strong> 
In self-archiving this collection of files and associated bibliographic 
metadata, I grant OAR@ICRISAT the right to store 
them and to make them permanently available publicly for free on-line. 
I declare that this material is my own intellectual property and I 
understand that OAR@ICRISAT does not assume any 
responsibility if there is any breach of copyright in distributing these 
files or metadata. (All authors are urged to prominently assert their 
copyright on the title page of their work.)</p>

<p xmlns="http://www.w3.org/1999/xhtml"><strong>For work being deposited by someone other than its 
author:</strong> I hereby declare that the collection of files and 
associated bibliographic metadata that I am archiving at 
OAR@ICRISAT) is in the public domain. If this is 
not the case, I accept full responsibility for any breach of copyright 
that distributing these files or metadata may entail.</p>

<p xmlns="http://www.w3.org/1999/xhtml">Clicking on the deposit button indicates your agreement to these 
terms.</p>
    </mods:useAndReproduction></mets:xmlData></mets:mdWrap></mets:rightsMD></mets:amdSec><mets:fileSec><mets:fileGrp USE="reference"><mets:file ID="eprint_10134_48001_1" SIZE="921485" OWNERID="http://oar.icrisat.org/10134/1/Heat-responsive-proteome.pdf" MIMETYPE="application/pdf"><mets:FLocat LOCTYPE="URL" xlink:type="simple" xlink:href="http://oar.icrisat.org/10134/1/Heat-responsive-proteome.pdf"></mets:FLocat></mets:file></mets:fileGrp></mets:fileSec><mets:structMap><mets:div DMDID="DMD_eprint_10134_mods" ADMID="TMD_eprint_10134"><mets:fptr FILEID="eprint_10134_document_48001_1"></mets:fptr></mets:div></mets:structMap></mets:mets>