AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains

Abstract FKBP53 is one of the seven multi-domain FK506-binding proteins present in Arabidopsis thaliana, and it is known to get targeted to the nucleus. It has a conserved PPIase domain at the C-terminus and a highly charged N-terminal stretch, which has been reported to bind to histone H3 and perfo...

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Bibliographic Details
Published in:Nucleic acids research 2020-02, Vol.48 (3), p.1531-1550
Main Authors: Singh, Ajit Kumar, Datta, Aritreyee, Jobichen, Chacko, Luan, Sheng, Vasudevan, Dileep
Format: Article
Language:English
Subjects:
Arabidopsis - chemistry
Arabidopsis - genetics
Arabidopsis Proteins - chemistry
Arabidopsis Proteins - genetics
Arabidopsis Proteins - ultrastructure
Binding Sites - genetics
Chromatin Assembly and Disassembly - genetics
Crystallography, X-Ray
Histones - chemistry
Histones - genetics
Molecular Chaperones - chemistry
Molecular Chaperones - genetics
Molecular Chaperones - ultrastructure
Nucleoplasmins - chemistry
Nucleoplasmins - genetics
Nucleosomes - chemistry
Nucleosomes - genetics
Peptidylprolyl Isomerase - genetics
Protein Binding - genetics
Protein Domains - genetics
Protein Folding
Structural Biology
Tacrolimus Binding Proteins - chemistry
Tacrolimus Binding Proteins - genetics
Tacrolimus Binding Proteins - ultrastructure
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Summary:Abstract FKBP53 is one of the seven multi-domain FK506-binding proteins present in Arabidopsis thaliana, and it is known to get targeted to the nucleus. It has a conserved PPIase domain at the C-terminus and a highly charged N-terminal stretch, which has been reported to bind to histone H3 and perform the function of a histone chaperone. To better understand the molecular details of this PPIase with histone chaperoning activity, we have solved the crystal structures of its terminal domains and functionally characterized them. The C-terminal domain showed strong PPIase activity, no role in histone chaperoning and revealed a monomeric five-beta palm-like fold that wrapped over a helix, typical of an FK506-binding domain. The N-terminal domain had a pentameric nucleoplasmin-fold; making this the first report of a plant nucleoplasmin structure. Further characterization revealed the N-terminal nucleoplasmin domain to interact with H2A/H2B and H3/H4 histone oligomers, individually, as well as simultaneously, suggesting two different binding sites for H2A/H2B and H3/H4. The pentameric domain assists nucleosome assembly and forms a discrete complex with pre-formed nucleosomes; wherein two pentamers bind to a nucleosome.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkz1153