The H3 chaperone function of NASP is conserved in Arabidopsis

Sammanfattning

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.

Nyckelord

histone; chaperone; chromatin; nucleosome; Arabidopsis thaliana

Publicerad i

Plant Journal
2016, volym: 88, nummer: 3, sidor: 425-436
Utgivare: Wiley-Blackwell

SLU författare

• Maksimov, Vladimir

  • Institutionen för växtbiologi, Sveriges lantbruksuniversitet
    

• Nakamura, Miyuki

  • Institutionen för växtbiologi, Sveriges lantbruksuniversitet
    

• Hennig, Lars

  • Institutionen för växtbiologi, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Cellbiologi
Evolutionsbiologi
Bioinformatik och systembiologi

Publikationens identifierare

• DOI: https://doi.org/10.1111/tpj.13263

Permanent länk till denna sida (URI)

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