Nucleosome assembly protein 1-like 1

Definition:

Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly. Participates also in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair. Stimulates also homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair. Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity).; (Microbial infection) Positively regulates Epstein-Barr virus reactivation in epithelial cells through the induction of viral BZLF1 expression.; (Microbial infection) Together with human herpesvirus 8 protein LANA1, assists the proper assembly of the nucleosome on the replicated viral DNA.

References:

[1]. Pawan Vinod Mehrotra, et al. DNA repair factor APLF is a histone chaperone. Mol Cell. 2011 Jan 7;41(1):46-55. [Content Brief]

[2]. Ju Yeon Lee, et al. NAP1L1 accelerates activation and decreases pausing to enhance nucleosome remodeling by CSB. Nucleic Acids Res. 2017 May 5;45(8):4696-4707. [Content Brief]

[3]. Mitsuru Okuwaki, et al. Functional characterization of human nucleosome assembly protein 1-like proteins as histone chaperones. Genes Cells. 2010 Jan;15(1):13-27. [Content Brief]

[4]. Shinichi Machida, et al. Nap1 stimulates homologous recombination by RAD51 and RAD54 in higher-ordered chromatin containing histone H1. Sci Rep. 2014 May 6;4:4863. [Content Brief]

[5]. Namrata Gupta, et al. KSHV encoded LANA recruits Nucleosome Assembly Protein NAP1L1 for regulating viral DNA replication and transcription. Sci Rep. 2016 Sep 7;6:32633. [Content Brief]

[6]. Hideaki Ohtomo, et al. C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4. Genes Cells. 2016 Mar;21(3):252-63. [Content Brief]

[7]. Sheila Mansouri, et al. A role for the nucleosome assembly proteins TAF-Iβ and NAP1 in the activation of BZLF1 expression and Epstein-Barr virus reactivation. PLoS One. 2013 May 14;8(5):e63802. [Content Brief]

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