{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["45"],"submitter":["Ogawa M"],"pubmed_abstract":["Small heat-shock proteins (sHsps) are ATP-independent chaperones whose oligomerization and client capture are regulated by a conserved C-terminal IXI/V motif. Here, we identify and characterize an sHsp from the marine cyanobacterium <i>Picosynechococcus</i> sp. NKBG15041c (NKBG-sHsp), which has an acidic C-terminal extension following IXI/V. We dissect the role of its acidic C-terminal extension using truncation mutants, one with the acidic C-terminal extension deleted (NKBG-sHspΔC), and another with both the acidic C-terminal extension and the IXI/V motif deleted (NKBG-sHspΔΔC). By size-exclusion chromatography by HPLC, NKBG-sHsp and NKBG-sHspΔC existed as large oligomers at 20 °C and reversibly dissociated into smaller species at 50 °C, whereas NKBG-sHspΔΔC remained a small oligomer with"],"journal":["Biochemistry and biophysics reports"],"pagination":["102500"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12925178"],"repository":["biostudies-literature"],"pubmed_title":["Structural and functional characterization of sHsp from the marine cyanobacterium &lt;i&gt;Picosynechococcus&lt;/i&gt; sp. NKBG15041c."],"pmcid":["PMC12925178"],"pubmed_authors":["Yohda M","Yamada A","Naka W","Inoue R","Ogawa M","Morishima K","Sugiyama M"],"additional_accession":[]},"is_claimable":false,"name":"Structural and functional characterization of sHsp from the marine cyanobacterium &lt;i&gt;Picosynechococcus&lt;/i&gt; sp. NKBG15041c.","description":"Small heat-shock proteins (sHsps) are ATP-independent chaperones whose oligomerization and client capture are regulated by a conserved C-terminal IXI/V motif. Here, we identify and characterize an sHsp from the marine cyanobacterium <i>Picosynechococcus</i> sp. NKBG15041c (NKBG-sHsp), which has an acidic C-terminal extension following IXI/V. We dissect the role of its acidic C-terminal extension using truncation mutants, one with the acidic C-terminal extension deleted (NKBG-sHspΔC), and another with both the acidic C-terminal extension and the IXI/V motif deleted (NKBG-sHspΔΔC). By size-exclusion chromatography by HPLC, NKBG-sHsp and NKBG-sHspΔC existed as large oligomers at 20 °C and reversibly dissociated into smaller species at 50 °C, whereas NKBG-sHspΔΔC remained a small oligomer with","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Mar","modification":"2026-07-16T18:48:39.603Z","creation":"2026-07-12T03:08:43.705Z"},"accession":"S-EPMC12925178","cross_references":{"pubmed":["41732416"],"doi":["10.1016/j.bbrep.2026.102500"]}}