Structural highlights
FunctionFKBPH_SCHPO PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Publication Abstract from PubMedHistone chaperones play significant roles in histone storage, transport, and assembly to form nucleosomes. Nucleoplasmin, a family of histone chaperones, has been reported from across the eukaryotic spectrum. Among these, the FK506-binding protein (FKBP) nucleoplasmin class, present in yeast, plants, and arthropods, possesses a nucleoplasmin core domain at the N-terminus, a central acidic stretch, and a characteristic C-terminal FKBP domain. CENP-A N-terminal domain isomerase 2 (Ani2) is an FKBP nucleoplasmin reported from the fission yeast, Schizosaccharomyces pombe. Ani2 has not been characterized in terms of its domain organization, chaperoning functions, and structural features. Herein, we undertook a domain-dissection approach and report the structural and in vitro functional attributes of Ani2. The N-terminal nucleoplasmin domain formed a pentamer, and the C-terminal domain (CTD) revealed a characteristic monomeric fold of an FKBP. The N-terminal domain (NTD) showed histone chaperone activity in vitro, and the FKBP domain functioned as a prolyl isomerase, confirming that this is a dual chaperone. Moreover, the CTD efficiently binds to the immunosuppressive compounds FK506 and rapamycin. Unravelling the structure-function features of Ani2, a dual chaperone from Schizosaccharomyces pombe.,Samal A, Patnaik P, Vasudevan D Int J Biol Macromol. 2026 Sep 15;383(Pt 1):154525. doi: , 10.1016/j.ijbiomac.2026.154525. PMID:42744269[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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