{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T08:08:10Z","timestamp":1782979690920,"version":"3.54.5"},"reference-count":47,"publisher":"The Company of Biologists","issue":"14","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,7,15]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1242\/jcs.115.14.2881","type":"journal-article","created":{"date-parts":[[2021,4,24]],"date-time":"2021-04-24T06:36:42Z","timestamp":1619246202000},"page":"2881-2891","source":"Crossref","is-referenced-by-count":17,"title":["A novel linker histone-like protein is associated with cytoplasmic filaments in<i>Caenorhabditis elegans<\/i>"],"prefix":"10.1242","volume":"115","author":[{"given":"Monika A.","family":"Jedrusik","sequence":"first","affiliation":[{"name":"Georg-August University of Go\u0308ttingen, Third Department of Zoology \u2014Developmental Biology, Humboldtallee 34A, 37073 Go\u0308ttingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Vogt","sequence":"additional","affiliation":[{"name":"Georg-August University of Go\u0308ttingen, Institute for X-ray Physics,Geiststra\u00dfe 11, 37073 Go\u0308ttingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Claus","sequence":"additional","affiliation":[{"name":"Hannover Medical School, Neuroanatomy, Carl-Neuberg-Str.1, 30625 Hannover,Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ekkehard","family":"Schulze","sequence":"additional","affiliation":[{"name":"Georg-August University of Go\u0308ttingen, Third Department of Zoology \u2014Developmental Biology, Humboldtallee 34A, 37073 Go\u0308ttingen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042517232856700_REF1","unstructured":"Albig, W., Meergans, T. and Doenecke, D.(1997). Characterization of the H1.5 gene completes the set of human H1 subtype genes. Gene184, 141-148."},{"key":"2021042517232856700_REF2","doi-asserted-by":"crossref","unstructured":"Altschul, S. F., Gish, D., Miller, W., Myers, E. W. and Lipman,D. J. (1990). Basic local alignment search tool.J. Mol. Biol.215, 403-410.","DOI":"10.1016\/S0022-2836(05)80360-2"},{"key":"2021042517232856700_REF3","doi-asserted-by":"crossref","unstructured":"Arion, D., Meijer, L., Brizuela, L. and Beach, L.(1988). cdc2 is a component of the M phase-specific histone H1 kinase: evidence for identity with MPF. Cell55, 371-378.","DOI":"10.1016\/0092-8674(88)90060-8"},{"key":"2021042517232856700_REF4","doi-asserted-by":"crossref","unstructured":"Bartnik, E., Osborn, M. and Weber, K. (1986). Intermediate filaments in the muscle and epithelial cells of nematodes.J. Cell Biol.102, 2033-2041.","DOI":"10.1083\/jcb.102.6.2033"},{"key":"2021042517232856700_REF5","doi-asserted-by":"crossref","unstructured":"Barra, J. L., Rhounim, L., Rossignol, J. L. and Faugeron, G.(2000). Histone H1 is dispensable for methylation-associated gene silencing in Ascobolus immersus and essential for long life span.Mol. Cell. Biol.20, 61-69.","DOI":"10.1128\/MCB.20.1.61-69.2000"},{"key":"2021042517232856700_REF6","doi-asserted-by":"crossref","unstructured":"Bateman, A., Birney, E., Durbin, R., Eddy, S. R., Howe, K. L. and Sonnhammer, E. L. (2000). The Pfam protein families database. Nucleic Acids Res.28, 263-266.","DOI":"10.1093\/nar\/28.1.263"},{"key":"2021042517232856700_REF7","doi-asserted-by":"crossref","unstructured":"Brenner, S. (1974). The genetics of Caenorhabditis elegans.Genetics77, 71-94.","DOI":"10.1093\/genetics\/77.1.71"},{"key":"2021042517232856700_REF8","doi-asserted-by":"crossref","unstructured":"Christensen, M. E. and Banker, N. (1992). Mapping of monoclonal antibody epitopes in the nucleolar protein fibrillarin(B-36) of Physarum polycephalum.Cell Biol. Int. Rep.16, 1119-1131.","DOI":"10.1016\/S0309-1651(05)80038-4"},{"key":"2021042517232856700_REF9","doi-asserted-by":"crossref","unstructured":"Clark, K. L., Halay, E. D., Lai, E. and Burley, S. K.(1993). Co-crystal structure of the HNF-3\/fork head DNA-recognition motif resembles histone H5. Nature364, 412-420.","DOI":"10.1038\/364412a0"},{"key":"2021042517232856700_REF10","doi-asserted-by":"crossref","unstructured":"Doenecke, D., Albig, W., Bouterfa, H. and Drabent, B.(1994). Organization and expression of H1 histone and H1 replacement histone genes. J. Cell Biochem.54, 423-431.","DOI":"10.1002\/jcb.240540409"},{"key":"2021042517232856700_REF11","doi-asserted-by":"crossref","unstructured":"Drabent, B., Franke, K., Bode, C., Kosciessa, U., Bouterfa, U. H., Hameister, H. and Doenecke, D. (1995). Isolation of two murine H1 histone genes and chromosomal mapping of the H1 gene complement.Mamm. Genome6, 505-511.","DOI":"10.1007\/BF00356166"},{"key":"2021042517232856700_REF12","doi-asserted-by":"crossref","unstructured":"Escher, D. and Schaffner, W. (1997). Gene activation at a distance and telomeric silencing are not affected by yeast histone H1. Mol. Gen. Genet.256, 456-461.","DOI":"10.1007\/s004380050589"},{"key":"2021042517232856700_REF13","doi-asserted-by":"crossref","unstructured":"Finney, M. and Ruvkun, G. (1990). The unc-86 gene product couples cell lineage and cell identity in C. elegans.Cell63, 895-905.","DOI":"10.1016\/0092-8674(90)90493-X"},{"key":"2021042517232856700_REF14","doi-asserted-by":"crossref","unstructured":"Fire, A., Xu, S., Montgomery, M. K., Kostas, S. A., Driver, S. E. and Mello, C. C. (1998). Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans.Nature391, 806-811.","DOI":"10.1038\/35888"},{"key":"2021042517232856700_REF15","doi-asserted-by":"crossref","unstructured":"Han, M., Chang, M., Kim, U. J. and Grunstein, M.(1987). Histone H2B repression causes cell-cycle-specific arrest in yeast: effects on chromosomal segregation, replication and transcription.Cell48, 589-597.","DOI":"10.1016\/0092-8674(87)90237-6"},{"key":"2021042517232856700_REF16","doi-asserted-by":"crossref","unstructured":"Henriquez, J. P., Casar, J. C., Fuentealba, L., Carey, D. J. and Brandan, E. (2002). Extracellular matrix histone H1 binds to perlecan, is present in regenerating skeletal muscle and stimulates myoblast proliferation. J. Cell Sci.115, 2041-2051.","DOI":"10.1242\/jcs.115.10.2041"},{"key":"2021042517232856700_REF17","doi-asserted-by":"crossref","unstructured":"Heald, R. and McKeon, F. (1990). Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell61, 579-589.","DOI":"10.1016\/0092-8674(90)90470-Y"},{"key":"2021042517232856700_REF18","unstructured":"Ishikawa, R., Kagami, O., Hayashi, C. and Kohama, K.(1992). The binding of nonmuscle caldesmon from brain to microtubules. Regulations by Ca(2+)-calmodulin and cdc2 kinase.FEBS-Lett.299, 54-56."},{"key":"2021042517232856700_REF19","unstructured":"Jedrusik, M. A. and Schulze, E. (2001). A single histone H1 isoform (H1.1) is essential for chromatin silencing and germline development in Caenorhabditis elegans.Development128, 1069-1080."},{"key":"2021042517232856700_REF20","doi-asserted-by":"crossref","unstructured":"Kaczanowski, S. and Jerzmanowski, A. (2001). Evolutionary correlation between linker histones and microtubulear structures.J. Mol. Evol.53, 19-30.","DOI":"10.1007\/s002390000000"},{"key":"2021042517232856700_REF21","doi-asserted-by":"crossref","unstructured":"Karabinos, A., Schmidt, H., Harborth, J., Schnabel, R. and Weber, K. (2001). Essential roles for four cytoplasmic intermediate filament proteins in Caenorhabditis elegans development.Proc. Natl. Acad. Sci. USA98, 7863-7868.","DOI":"10.1073\/pnas.121169998"},{"key":"2021042517232856700_REF22","unstructured":"Kelley, L. A., MacCallum, R. M. and Sternberg, M. J. E.(2000). Enhanced Genome Annotation using Structural Profiles in the Program 3D-PSSM. J. Mol. Biol.299, 499-520."},{"key":"2021042517232856700_REF23","doi-asserted-by":"crossref","unstructured":"Kim, U. J., Han, M., Kayne, P. and Grunstein, M.(1988). Effects of histone H4 depletion on the cell cycle and transcription of Saccharomyces cerevisiae.EMBO J.7, 2211-2219.","DOI":"10.1002\/j.1460-2075.1988.tb03060.x"},{"key":"2021042517232856700_REF24","doi-asserted-by":"crossref","unstructured":"Kramer, J. M., French, R. P., Park, E. C. and Johnson, J. J.(1990). The Caenorhabditis elegans rol-6 gene, which interacts with the sqt-1 collagen gene to determine organismal morphology, encodes a collagen. Mol. Cell. Biol.10, 2081-2089.","DOI":"10.1128\/MCB.10.5.2081"},{"key":"2021042517232856700_REF25","unstructured":"Lever, M. A., Th'ng, J. P., Sun, X. and Hendzel, M. J.(2000). Rapid exchange of histone H1.1 on chromatin in living human cells. Nature408, 873-876."},{"key":"2021042517232856700_REF26","doi-asserted-by":"crossref","unstructured":"Liu, J., Ben-Shahar, T. R., Riemer, D., Treinin, M., Spann, P.,Weber, K., Fire, A. and Gruenbaum, Y. (2000). Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression and spatial organization of nuclear pore complexes.Mol. Biol. Cell11, 3937-3947.","DOI":"10.1091\/mbc.11.11.3937"},{"key":"2021042517232856700_REF27","unstructured":"Mello, C. C., Kramer, J. M., Stinchcomb, D. and Ambros, V.(1991). Efficient gene transfer in C. elegans:extrachromosomal maintenance and integration of transforming sequences.EMBO J.10, 3959-3970."},{"key":"2021042517232856700_REF28","doi-asserted-by":"crossref","unstructured":"Miller, D. M. and Shakes, D. C. (1995). Immunofluorescence microscopy. Methods Cell Biol.48, 365-394.","DOI":"10.1016\/S0091-679X(08)61396-5"},{"key":"2021042517232856700_REF29","doi-asserted-by":"crossref","unstructured":"Misteli, T., Gunjan, A., Hock, R., Bustin, M. and Brown, D. T. (2000). Dynamic binding of histone H1 to chromatin in living cells. Nature408, 877-881.","DOI":"10.1038\/35048610"},{"key":"2021042517232856700_REF30","doi-asserted-by":"crossref","unstructured":"Multigner, L., Gagnon, J. and Van-Dorsselar, T.(1992). Stabilization of sea urchin flagellar microtubules by histone H1. Nature360, 33-39.","DOI":"10.1038\/360033a0"},{"key":"2021042517232856700_REF31","doi-asserted-by":"crossref","unstructured":"Prymakowska-Bosak, M., Przewloka, M. R., Iwkiewicz, J.,Egierszdorff, S., Kuras, M., Chaubet, N., Gigot, C., Spiker, S. and Jerzmanowski, A. (1996). Histone H1 overexpressed to high level in tobacco affects certain developmental programs but has limited effect on basal cellular functions. Proc. Natl. Acad. Sci. USA.93, 1250-1255.","DOI":"10.1073\/pnas.93.19.10250"},{"key":"2021042517232856700_REF32","doi-asserted-by":"crossref","unstructured":"Prymakowska-Bosak, M., Przewloka, M. R., Slusarczyk, J., Kuras,M., Lichota, J., Kilianczyk, B. and Jerzmanowski, A. (1999). Linker histones play a role in male meiosis and the development of pollen grains in tobacco. Plant Cell11, 2317-2329.","DOI":"10.1105\/tpc.11.12.2317"},{"key":"2021042517232856700_REF33","doi-asserted-by":"crossref","unstructured":"Ramakrishnan, V. (1997). Histone H1 and chromatin higher-order structure. Crit. Rev. Eukaryot. Gene Expr.7, 215-230.","DOI":"10.1615\/CritRevEukarGeneExpr.v7.i3.20"},{"key":"2021042517232856700_REF34","doi-asserted-by":"crossref","unstructured":"Ramon, A., Muro-Pastor, M. I., Scazzocchio, C. and Gonzalez,R. (2000). Deletion of the unique gene encoding a typical histone H1 has no apparent phenotype in Aspergillus nidulans.Mol. Microbiol.35, 223-233.","DOI":"10.1046\/j.1365-2958.2000.01702.x"},{"key":"2021042517232856700_REF35","doi-asserted-by":"crossref","unstructured":"Rosenberg, A. H., Lade, B. N., Chui, D. S., Lin, S. W., Dunn, S. W. and Studier, F. W. (1987). Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene56, 125-135.","DOI":"10.1016\/0378-1119(87)90165-X"},{"key":"2021042517232856700_REF36","doi-asserted-by":"crossref","unstructured":"Shen, X., Yu, L., Weir, J. W. and Gorovsky, M. A.(1995). Linker histones are not essential and affect chromatin condensation in vivo. Cell82, 47-56.","DOI":"10.1016\/0092-8674(95)90051-9"},{"key":"2021042517232856700_REF37","doi-asserted-by":"crossref","unstructured":"Sobue, K., Muramoto, Y., Fujita, M. and Kakiuchi, S.(1981). Purification of a calmodulin-binding protein from chicken gizzard that interacts with Factin. Proc. Natl. Acad. Sci. USA78, 5652-5655.","DOI":"10.1073\/pnas.78.9.5652"},{"key":"2021042517232856700_REF38","doi-asserted-by":"crossref","unstructured":"Strome, S. and Wood, W. B. (1982). Immunofluorescence visualization of germ-line-specific cytoplasmic granules in embryos, larvae, and adults of Caenorhabditis elegans.Proc. Natl. Acad. Sci. USA79, 1558-1562.","DOI":"10.1073\/pnas.79.5.1558"},{"key":"2021042517232856700_REF39","doi-asserted-by":"crossref","unstructured":"Subirana, J. A. (1990). Analysis of the charge distribution in the C-terminal region of histone H1 as related to its interaction with DNA. Biopolymers29, 1351-1357.","DOI":"10.1002\/bip.360291003"},{"key":"2021042517232856700_REF40","unstructured":"Sulston, J. and Hodgkin, J. (1988). Methods. InThe Nematode Caenorhabditis elegans (ed. W. B. Wood),pp. 587-606. New York: Cold Spring Harbour Laboratory Press."},{"key":"2021042517232856700_REF41","doi-asserted-by":"crossref","unstructured":"Tanaka, I., Akahori, Y., Gomi, K., Suzuki, T. and Ueda, K.(1999). A novel histone variant localized in nucleoli of higher plant cells. Chromosoma108, 190-199.","DOI":"10.1007\/s004120050368"},{"key":"2021042517232856700_REF42","doi-asserted-by":"crossref","unstructured":"Timmons, L. and Fire, A. (1998). Specific interference by ingested dsRNA. Nature395, 854.","DOI":"10.1038\/27579"},{"key":"2021042517232856700_REF43","doi-asserted-by":"crossref","unstructured":"Towbin, H., Staehelin, T. and Gordon, J.(1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proc. Natl. Acad. Sci. USA76, 4350-4354.","DOI":"10.1073\/pnas.76.9.4350"},{"key":"2021042517232856700_REF44","doi-asserted-by":"crossref","unstructured":"Tsujimura, K., Ogawara, M., Takeuchi, Y., Imajoh-Ohmi, S., Ha,M. H. and Inagaki, M. (1994). Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis. J. Biol. Chem.269, 31097-31106.","DOI":"10.1016\/S0021-9258(18)47395-4"},{"key":"2021042517232856700_REF45","doi-asserted-by":"crossref","unstructured":"Wisniewski, J. R. and Schulze, E. (1994). High affinity interaction of dipteran high mobility group (HMG) proteins 1 with DNA is modulated by COOH-terminal regions flanking the HMG box domain.J. Biol. Chem.269, 10713-10719.","DOI":"10.1016\/S0021-9258(17)34117-0"},{"key":"2021042517232856700_REF46","doi-asserted-by":"crossref","unstructured":"Yamamoto, T. and Horikoshi, M. (1996). Cloning of the cDNA encoding a novel subtype of histone H1.Gene.173, 281-285.","DOI":"10.1016\/0378-1119(96)00020-0"},{"key":"2021042517232856700_REF47","doi-asserted-by":"crossref","unstructured":"Yamashiro, S., Yamakita, Y., Hosoya, H. and Matsumura, F.(1991). Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis. Nature349, 169-172.","DOI":"10.1038\/349169a0"}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/115\/14\/2881\/1473665\/2881.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/115\/14\/2881\/1473665\/2881.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,5,2]],"date-time":"2021-05-02T10:29:26Z","timestamp":1619951366000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/115\/14\/2881\/26780\/A-novel-linker-histone-like-protein-is-associated"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,7,15]]},"references-count":47,"journal-issue":{"issue":"14","published-print":{"date-parts":[[2002,7,15]]}},"URL":"https:\/\/doi.org\/10.1242\/jcs.115.14.2881","relation":{},"ISSN":["1477-9137","0021-9533"],"issn-type":[{"value":"1477-9137","type":"electronic"},{"value":"0021-9533","type":"print"}],"subject":[],"published":{"date-parts":[[2002,7,15]]}}}