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==== | ==Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1)== | ||
<StructureSection load='7c7x' size='340' side='right'caption='[[7c7x]]' scene=''> | <StructureSection load='7c7x' size='340' side='right'caption='[[7c7x]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[7c7x]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C7X FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7c7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c7x OCA], [https://pdbe.org/7c7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c7x RCSB], [https://www.ebi.ac.uk/pdbsum/7c7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c7x ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/H2A6_ARATH H2A6_ARATH] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for the T-DNA integration step of plant transformation by Agrobacterium. May play an important role in illegitimate recombination.<ref>PMID:10639185</ref> <ref>PMID:12410808</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nucleosome Assembly Protein 1 (NAP1) family proteins are evolutionarily conserved histone chaperones that play important roles in diverse biological processes. In this study, we determined the crystal structure of Arabidopsis NAP1-Related Protein 1 (NRP1) complexed with H2A-H2B and uncovered a previously unknown interaction mechanism in histone chaperoning. Both in vitro binding and in vivo plant rescue assays proved that interaction mediated by the N-terminal alpha-helix (alphaN) domain is essential for NRP1 function. In addition, the C-terminal acidic domain (CTAD) of NRP1 binds to H2A-H2B through a conserved mode similar to other histone chaperones. We further extended previous knowledge of the NAP1-conserved earmuff domain by mapping the amino acids of NRP1 involved in association with H2A-H2B. Finally, we showed that H2A-H2B interactions mediated by alphaN, earmuff, and CTAD domains are all required for the effective chaperone activity of NRP1. Collectively, our results reveal multiple interaction modes of a NAP1 family histone chaperone and shed light on how histone chaperones shield H2A-H2B from nonspecific interaction with DNA. | |||
NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B.,Luo Q, Wang B, Wu Z, Jiang W, Wang Y, Du K, Zhou N, Zheng L, Gan J, Shen WH, Ma J, Dong A Proc Natl Acad Sci U S A. 2020 Dec 1;117(48):30391-30399. doi: , 10.1073/pnas.2011089117. Epub 2020 Nov 16. PMID:33199628<ref>PMID:33199628</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7c7x" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Baihui W]] | ||
[[Category: Luo Q]] | |||
Latest revision as of 18:58, 29 November 2023
Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1)Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1)
Structural highlights
FunctionH2A6_ARATH Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for the T-DNA integration step of plant transformation by Agrobacterium. May play an important role in illegitimate recombination.[1] [2] Publication Abstract from PubMedNucleosome Assembly Protein 1 (NAP1) family proteins are evolutionarily conserved histone chaperones that play important roles in diverse biological processes. In this study, we determined the crystal structure of Arabidopsis NAP1-Related Protein 1 (NRP1) complexed with H2A-H2B and uncovered a previously unknown interaction mechanism in histone chaperoning. Both in vitro binding and in vivo plant rescue assays proved that interaction mediated by the N-terminal alpha-helix (alphaN) domain is essential for NRP1 function. In addition, the C-terminal acidic domain (CTAD) of NRP1 binds to H2A-H2B through a conserved mode similar to other histone chaperones. We further extended previous knowledge of the NAP1-conserved earmuff domain by mapping the amino acids of NRP1 involved in association with H2A-H2B. Finally, we showed that H2A-H2B interactions mediated by alphaN, earmuff, and CTAD domains are all required for the effective chaperone activity of NRP1. Collectively, our results reveal multiple interaction modes of a NAP1 family histone chaperone and shed light on how histone chaperones shield H2A-H2B from nonspecific interaction with DNA. NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B.,Luo Q, Wang B, Wu Z, Jiang W, Wang Y, Du K, Zhou N, Zheng L, Gan J, Shen WH, Ma J, Dong A Proc Natl Acad Sci U S A. 2020 Dec 1;117(48):30391-30399. doi: , 10.1073/pnas.2011089117. Epub 2020 Nov 16. PMID:33199628[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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