Unknown

Dataset Information

0

Internuclear diffusion of histone H1 within cellular compartments of Aspergillus nidulans.


ABSTRACT: Histone H1 is an evolutionarily conserved linker histone protein that functions in arranging and stabilizing chromatin structure and is frequently fused to a fluorescent protein to track nuclei in live cells. In time-lapse analyses, we observed stochastic exchange of photoactivated Dendra2-histone H1 protein between nuclei within the same cellular compartment. We also observed exchange of histones between genetically distinct nuclei in a heterokaryon derived from fusion of strains carrying histone H1-RFP or H1-GFP. Subsequent analysis of the resulting uninucleate conidia containing both RFP- and GFP-labeled histone H1 proteins showed only parental genotypes, ruling out genetic recombination and diploidization. These data together suggest that the linker histone H1 protein can diffuse between non-daughter nuclei in the filamentous fungus Aspergillus nidulans.

SUBMITTER: Mela AP 

PROVIDER: S-EPMC6095493 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

altmetric image

Publications

Internuclear diffusion of histone H1 within cellular compartments of Aspergillus nidulans.

Mela Alexander P AP   Momany Michelle M  

PloS one 20180816 8


Histone H1 is an evolutionarily conserved linker histone protein that functions in arranging and stabilizing chromatin structure and is frequently fused to a fluorescent protein to track nuclei in live cells. In time-lapse analyses, we observed stochastic exchange of photoactivated Dendra2-histone H1 protein between nuclei within the same cellular compartment. We also observed exchange of histones between genetically distinct nuclei in a heterokaryon derived from fusion of strains carrying histo  ...[more]

Similar Datasets

| S-EPMC5711018 | biostudies-literature
| S-EPMC2064697 | biostudies-literature
| S-EPMC3542395 | biostudies-literature
| S-EPMC3811361 | biostudies-literature
| S-EPMC8351559 | biostudies-literature
| S-EPMC3514908 | biostudies-literature
| S-EPMC98905 | biostudies-literature
| S-EPMC1693977 | biostudies-literature
| S-EPMC7493923 | biostudies-literature
| S-EPMC7705104 | biostudies-literature