The H3 chaperone function of NASP is conserved in Arabidopsis

Vladimir Maksimov; Miyuki Nakamura; Thomas Wildhaber; Paolo Nanni; Margareta Ramström; Jonas Bergquist; Lars Hennig

doi:10.1111/tpj.13263

The H3 chaperone function of NASP is conserved in Arabidopsis

Vladimir Maksimov
, Miyuki Nakamura
, Thomas Wildhaber
, Paolo Nanni
, Margareta Ramström
, Jonas Bergquist
, Lars Hennig

Department of Plant Biology

Publication: Contribution to journal › Journal article › peer-review

Abstract

Histones are abundant cellular proteins but, if not incorporated into chromatin, they are usually bound by histone chaperones. Here, we identify Arabidopsis NASP as a chaperone for histones H3.1 and H3.3. NASP interacts invitro with monomeric H3.1 and H3.3 as well as with histone H3.1-H4 and H3.3-H4 dimers. However, NASP does not bind to monomeric H4. NASP shifts the equilibrium between histone dimers and tetramers towards tetramers but does not interact with tetramers invitro. Arabidopsis NASP promotes [H3-H4](2) tetrasome formation, possibly by providing preassembled histone tetramers. However, NASP does not promote disassembly of invitro preassembled tetrasomes. In contrast to its mammalian homolog, Arabidopsis NASP is a predominantly nuclear protein. In vivo, NASP binds mainly monomeric H3.1 and H3.3. Pulldown experiments indicated that NASP may also interact with the histone chaperone MSI1 and a HSC70 heat shock protein.

Original language	English
Pages (from-to)	425-436
Number of pages	12
Journal	Plant Journal
Volume	88
Issue number	3
DOIs	https://doi.org/10.1111/tpj.13263
Publication status	Published - 2016

Keywords

histone
chaperone
chromatin
nucleosome
Arabidopsis thaliana

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10.1111/tpj.13263

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title = "The H3 chaperone function of NASP is conserved in Arabidopsis",

abstract = "Histones are abundant cellular proteins but, if not incorporated into chromatin, they are usually bound by histone chaperones. Here, we identify Arabidopsis NASP as a chaperone for histones H3.1 and H3.3. NASP interacts invitro with monomeric H3.1 and H3.3 as well as with histone H3.1-H4 and H3.3-H4 dimers. However, NASP does not bind to monomeric H4. NASP shifts the equilibrium between histone dimers and tetramers towards tetramers but does not interact with tetramers invitro. Arabidopsis NASP promotes [H3-H4](2) tetrasome formation, possibly by providing preassembled histone tetramers. However, NASP does not promote disassembly of invitro preassembled tetrasomes. In contrast to its mammalian homolog, Arabidopsis NASP is a predominantly nuclear protein. In vivo, NASP binds mainly monomeric H3.1 and H3.3. Pulldown experiments indicated that NASP may also interact with the histone chaperone MSI1 and a HSC70 heat shock protein.",

keywords = "histone, chaperone, chromatin, nucleosome, Arabidopsis thaliana, histone, chaperone, chromatin, nucleosome, Arabidopsis thaliana",

author = "Vladimir Maksimov and Miyuki Nakamura and Thomas Wildhaber and Paolo Nanni and Margareta Ramstr{\"o}m and Jonas Bergquist and Lars Hennig",

year = "2016",

doi = "10.1111/tpj.13263",

language = "English",

volume = "88",

pages = "425--436",

journal = "Plant Journal",

issn = "0960-7412",

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T1 - The H3 chaperone function of NASP is conserved in Arabidopsis

AU - Maksimov, Vladimir

AU - Nakamura, Miyuki

AU - Wildhaber, Thomas

AU - Nanni, Paolo

AU - Ramström, Margareta

AU - Bergquist, Jonas

AU - Hennig, Lars

PY - 2016

Y1 - 2016

N2 - Histones are abundant cellular proteins but, if not incorporated into chromatin, they are usually bound by histone chaperones. Here, we identify Arabidopsis NASP as a chaperone for histones H3.1 and H3.3. NASP interacts invitro with monomeric H3.1 and H3.3 as well as with histone H3.1-H4 and H3.3-H4 dimers. However, NASP does not bind to monomeric H4. NASP shifts the equilibrium between histone dimers and tetramers towards tetramers but does not interact with tetramers invitro. Arabidopsis NASP promotes [H3-H4](2) tetrasome formation, possibly by providing preassembled histone tetramers. However, NASP does not promote disassembly of invitro preassembled tetrasomes. In contrast to its mammalian homolog, Arabidopsis NASP is a predominantly nuclear protein. In vivo, NASP binds mainly monomeric H3.1 and H3.3. Pulldown experiments indicated that NASP may also interact with the histone chaperone MSI1 and a HSC70 heat shock protein.

AB - Histones are abundant cellular proteins but, if not incorporated into chromatin, they are usually bound by histone chaperones. Here, we identify Arabidopsis NASP as a chaperone for histones H3.1 and H3.3. NASP interacts invitro with monomeric H3.1 and H3.3 as well as with histone H3.1-H4 and H3.3-H4 dimers. However, NASP does not bind to monomeric H4. NASP shifts the equilibrium between histone dimers and tetramers towards tetramers but does not interact with tetramers invitro. Arabidopsis NASP promotes [H3-H4](2) tetrasome formation, possibly by providing preassembled histone tetramers. However, NASP does not promote disassembly of invitro preassembled tetrasomes. In contrast to its mammalian homolog, Arabidopsis NASP is a predominantly nuclear protein. In vivo, NASP binds mainly monomeric H3.1 and H3.3. Pulldown experiments indicated that NASP may also interact with the histone chaperone MSI1 and a HSC70 heat shock protein.

KW - histone

KW - chaperone

KW - chromatin

KW - nucleosome

KW - Arabidopsis thaliana

KW - histone

KW - chaperone

KW - chromatin

KW - nucleosome

KW - Arabidopsis thaliana

UR - https://res.slu.se/id/publ/81017

U2 - 10.1111/tpj.13263

DO - 10.1111/tpj.13263

M3 - Journal article

C2 - 27402088

SN - 0960-7412

VL - 88

SP - 425

EP - 436

JO - Plant Journal

JF - Plant Journal

IS - 3

ER -

The H3 chaperone function of NASP is conserved in Arabidopsis

Abstract

Keywords

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