Structural and functional characterization of sHsp from the marine cyanobacterium <i>Picosynechococcus</i> sp. NKBG15041c.

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 Picosynechococcus 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

SUBMITTER: Ogawa M 

PROVIDER: S-EPMC12925178 | biostudies-literature | 2026 Mar

REPOSITORIES: biostudies-literature