Structural highlights
Function
CPY71_ARATH PPIases accelerate the folding of proteins (Probable). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:33098102). Histone proline isomerase that increases the rate of cis-trans isomerization of the synthetic histone H3 peptides H3P30 (RKSAP30F-p-nitroanilide) and H3P30K27me3 (RKme3-SAP30F-p-nitroanilide) in the histone H3 N-terminal tail, in vitro (PubMed:33098102). Histone remodeling factor involved in chromatin-based gene silencing (PubMed:17704213). Reinforces H3K27 methylation (PubMed:17704213). Involved in fundamental processes of chromatin assembly and histone modification by mediating the targeting of FAS1 and LHP1 on the chromatin (PubMed:21596687). Required for the formation and development of leaves, for normal phyllotaxy and for the formation, maintenance and activity of root and shoot apical meristems (PubMed:17704213).[1] [2] [3] [4] [5]
Publication Abstract from PubMed
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 A 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.
Structural and functional analyses of the PPIase domain of Arabidopsis thaliana CYP71 reveal its catalytic activity toward histone H3.,Lakhanpal S, Fan JS, Luan S, Swaminathan K FEBS Lett. 2020 Oct 23. doi: 10.1002/1873-3468.13965. PMID:33098102[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li H, He Z, Lu G, Lee SC, Alonso J, Ecker JR, Luan S. A WD40 domain cyclophilin interacts with histone H3 and functions in gene repression and organogenesis in Arabidopsis. Plant Cell. 2007 Aug;19(8):2403-16. PMID:17704213 doi:10.1105/tpc.107.053579
- ↑ Li H, Luan S. The cyclophilin AtCYP71 interacts with CAF-1 and LHP1 and functions in multiple chromatin remodeling processes. Mol Plant. 2011 Jul;4(4):748-58. PMID:21596687 doi:10.1093/mp/ssr036
- ↑ Lakhanpal S, Fan JS, Luan S, Swaminathan K. Structural and functional analyses of the PPIase domain of Arabidopsis thaliana CYP71 reveal its catalytic activity toward histone H3. FEBS Lett. 2021 Jan;595(1):145-154. PMID:33098102 doi:10.1002/1873-3468.13965
- ↑ Li H, He Z, Lu G, Lee SC, Alonso J, Ecker JR, Luan S. A WD40 domain cyclophilin interacts with histone H3 and functions in gene repression and organogenesis in Arabidopsis. Plant Cell. 2007 Aug;19(8):2403-16. PMID:17704213 doi:10.1105/tpc.107.053579
- ↑ Li H, Luan S. The cyclophilin AtCYP71 interacts with CAF-1 and LHP1 and functions in multiple chromatin remodeling processes. Mol Plant. 2011 Jul;4(4):748-58. PMID:21596687 doi:10.1093/mp/ssr036
- ↑ Lakhanpal S, Fan JS, Luan S, Swaminathan K. Structural and functional analyses of the PPIase domain of Arabidopsis thaliana CYP71 reveal its catalytic activity toward histone H3. FEBS Lett. 2021 Jan;595(1):145-154. PMID:33098102 doi:10.1002/1873-3468.13965
