Structural and functional analyses of the PPIase domain of Arabidopsis thaliana CYP71 reveal its catalytic activity toward histone H3

• Published in: FEBS letters Vol. 595; no. 1; pp. 145 - 154
• Main Authors: Lakhanpal, Smarth, Fan, Jing‐Song, Luan, Sheng, Swaminathan, Kunchithapadam
• Format: Journal Article
• Language: English
• Published: England 01.01.2021
• Subjects: arabidopsis; CYP71; genetic remodelling; PPIASE; proline isomerisation; shoot apical meristem; structural biology; proline isomerisation; PPIASE; shoot apical meristem; genetic remodelling; structural biology; CYP71; arabidopsis
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1002/1873-3468.13965

Arabidopsis thaliana CYP71 (AtCYP71) is a chromatin‐remodeling protein that promotes shoot apical meristem (SAM) differentiation. The N terminus of AtCYP71 contains a noncanonical WD domain, and the C terminus contains an enzymatic peptidyl‐prolyl isomerase (PPIase) cyclophilin (CYP) domain. To date, there has been no characterization of CYP71, and its mode of action remains unknown. Here, we report the crystal structure of the CYP domain of AtCYP71 at 1.9 Å resolution. The structure shows key differences when compared to the canonical CYP fold of human CypA. To the best our knowledge, this is the first A. thaliana CYP structure with a conserved active site loop. Using nuclear magnetic resonance spectroscopy, we demonstrate that the CYP domain is active toward histone H3. Our findings suggest that the PPIase activity of the CYP domain is important for the function of AtCYP71 in chromatin remodeling during organogenesis.