An archaeal histone-like protein regulates gene expression in response to salt stress

Author:

Sakrikar Saaz12,Schmid Amy K123ORCID

Affiliation:

1. Biology Department, Duke University, Durham, NC27708, USA

2. University Program in Genetics and Genomics, Duke University, Durham, NC27708, USA

3. Center for Genomics and Computational Biology, Duke University, Durham, NC27708, USA

Abstract

Abstract Histones, ubiquitous in eukaryotes as DNA-packing proteins, find their evolutionary origins in archaea. Unlike the characterized histone proteins of a number of methanogenic and themophilic archaea, previous research indicated that HpyA, the sole histone encoded in the model halophile Halobacterium salinarum, is not involved in DNA packaging. Instead, it was found to have widespread but subtle effects on gene expression and to maintain wild type cell morphology. However, the precise function of halophilic histone-like proteins remain unclear. Here we use quantitative phenotyping, genetics, and functional genomics to investigate HpyA function. These experiments revealed that HpyA is important for growth and rod-shaped morphology in reduced salinity. HpyA preferentially binds DNA at discrete genomic sites under low salt to regulate expression of ion uptake, particularly iron. HpyA also globally but indirectly activates other ion uptake and nucleotide biosynthesis pathways in a salt-dependent manner. Taken together, these results demonstrate an alternative function for an archaeal histone-like protein as a transcriptional regulator, with its function tuned to the physiological stressors of the hypersaline environment.

Funder

NSF

NIH

Publisher

Oxford University Press (OUP)

Subject

Genetics

Reference80 articles.

1. Phylogenomics of the nucleosome;Malik;Nat. Struct. Mol. Biol.,2003

2. Archaeal histone contributions to the origin of eukaryotes;Brunk;Trends Microbiol.,2019

3. Archaeal histones and the origin of the histone fold;Sandman;Curr. Opin. Microbiol.,2006

4. Histone variants -- ancient wrap artists of the epigenome;Talbert;Nat. Rev. Mol. Cell Biol.,2010

5. Histone structure and nucleosome stability;Mariño-Ramírez;Expert Rev. Proteomics,2005

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