PMID- 34551067
OWN - NLM
STAT- MEDLINE
DCOM- 20220207
LR  - 20220331
IS  - 1756-2651 (Electronic)
IS  - 0021-924X (Linking)
VI  - 170
IP  - 6
DP  - 2022 Jan 7
TI  - Nucleosome assembly protein 1 is a regulator of histone H1 acetylation.
PG  - 763-773
LID - 10.1093/jb/mvab098 [doi]
AB  - Acetylation of histone H1 is generally considered to activate transcription, 
      whereas deacetylation of H1 represses transcription. However, the precise 
      mechanism of the acetylation is unknown. Here, using chromatography, we 
      identified nucleosome assembly protein 1 (NAP-1) as having inhibitory activity 
      against histone H1 acetylation by acetyltransferase p300. We found that native 
      NAP-1 interacts with H1 in a Drosophila crude extract. We also found that it 
      inhibits the deacetylation of histone H1 by histone deacetylase 1. The core 
      histones in nucleosomes were acetylated in a GAL4-VP16 transcriptional 
      activator-dependent manner in vitro. This acetylation was strongly repressed by 
      hypoacetylated H1 but to a lesser extent by hyperacetylated H1. Consistent with 
      these findings, a micrococcal nuclease assay indicated that hypoacetylated H1, 
      which represses activator-dependent acetylation, was incorporated into chromatin, 
      whereas hyperacetylated H1 was not. To determine the contribution of NAP-1 to 
      transcriptional regulation in vivo, we compared NAP-1 knockdown (KD) with 
      coactivator CREB-binding protein (CBP) KD using RNA sequencing in Drosophila 
      Schneider 2 cells. Most genes were downregulated rather than upregulated by NAP-1 
      KD, and those downregulated genes were also downregulated by CBP KD. Our results 
      suggest that NAP-1 plays a role in transcriptional regulation by fine-tuning the 
      acetylation of histone H1. Graphical Abstract.
CI  - (c) The Author(s) 2021. Published by Oxford University Press on behalf of the 
      Japanese Biochemical Society. All rights reserved.
FAU - Yoneda, Mitsuhiro
AU  - Yoneda M
FAU - Yasui, Kiyoshi
AU  - Yasui K
FAU - Nakagawa, Takeya
AU  - Nakagawa T
FAU - Hattori, Naoko
AU  - Hattori N
FAU - Ito, Takashi
AU  - Ito T
LA  - eng
GR  - JP17H04044/Japan Society for the Promotion of Science/
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Drosophila Proteins)
RN  - 0 (GAL4 protein, Drosophila)
RN  - 0 (Histones)
RN  - 0 (Nap1 protein, Drosophila)
RN  - 0 (Nucleosome Assembly Protein 1)
RN  - 0 (Transcription Factors)
SB  - IM
EIN - J Biochem. 2022 Mar 31;171(4):467. PMID: 35137094
MH  - Acetylation
MH  - Animals
MH  - Drosophila Proteins/genetics/*metabolism
MH  - Drosophila melanogaster
MH  - HeLa Cells
MH  - Histones/genetics/*metabolism
MH  - Humans
MH  - Nucleosome Assembly Protein 1/genetics/*metabolism
MH  - Transcription Factors/genetics/metabolism
OTO - NOTNLM
OT  - histone acetylationhistone deacetylase 1 (HDAC1)linker histone H1NAP-1p300
EDAT- 2021/09/23 06:00
MHDA- 2022/02/08 06:00
CRDT- 2021/09/22 17:30
PHST- 2021/05/10 00:00 [received]
PHST- 2021/09/14 00:00 [accepted]
PHST- 2021/09/23 06:00 [pubmed]
PHST- 2022/02/08 06:00 [medline]
PHST- 2021/09/22 17:30 [entrez]
AID - 6373819 [pii]
AID - 10.1093/jb/mvab098 [doi]
PST - ppublish
SO  - J Biochem. 2022 Jan 7;170(6):763-773. doi: 10.1093/jb/mvab098.