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Journal of Cell Science 115, 2881-2891 (2002)
© 2002 The Company of Biologists Limited

Research Article

A novel linker histone-like protein is associated with cytoplasmic filaments in Caenorhabditis elegans

Monika A. Jedrusik1, Stefan Vogt2, Peter Claus3 and Ekkehard Schulze1,*

1 Georg-August University of Göttingen, Third Department of Zoology — Developmental Biology, Humboldtallee 34A, 37073 Göttingen, Germany
2 Georg-August University of Göttingen, Institute for X-ray Physics, Geiststraße 11, 37073 Göttingen, Germany
3 Hannover Medical School, Neuroanatomy, Carl-Neuberg-Str.1, 30625 Hannover, Germany

* Author for correspondence (e-mail: eschulz{at}gwdg.de )

Accepted 1 May 2002

The histone H1 complement of Caenorhabditis elegans contains a single unusual protein, H1.X. Although H1.X possesses the globular domain and the canonical three-domain structure of linker histones, the amino acid composition of H1.X is distinctly different from conventional linker histones in both terminal domains. We have characterized H1.X in C. elegans by antibody labeling, green fluorescent protein fusion protein expression and RNA interference. Unlike normal linker histones, H1.X is a cytoplasmic as well as a nuclear protein and is not associated with chromosomes. H1.X is most prominently expressed in the marginal cells of the pharynx and is associated with a peculiar cytoplasmic cytoskeletal structure therein, the tonofilaments. Additionally H1.X::GFP is expressed in the cytoplasm of body and vulva muscle cells, neurons, excretory cells and in the nucleoli of embryonic blastomeres and adult gut cells. RNA interference with H1.X results in uncoordinated and egg laying defective animals, as well as in a longitudinally enlarged pharynx. These phenotypes indicate a cytoplasmic role of H1.X in muscle growth and muscle function.

Key words: Caenorhabditis elegans, Histone H1, Chromatin, Intermediate filaments, Linker histone


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© The Company of Biologists Ltd 2002