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Hoyer-Fender, Sigrid
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Hoyer-Fender, Sigrid
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Hoyer-Fender, Sigrid
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Hoyer-Fender, S.
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2004Journal Article [["dc.bibliographiccitation.firstpage","189"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","198"],["dc.bibliographiccitation.volume","117"],["dc.contributor.author","Hoyer-Fender, Sigrid"],["dc.contributor.author","Czirr, E."],["dc.contributor.author","Radde, R."],["dc.contributor.author","Turner, JMA"],["dc.contributor.author","Mahadevaiah, S. K."],["dc.contributor.author","Pehrson, John R."],["dc.contributor.author","Burgoyne, P. S."],["dc.date.accessioned","2018-11-07T10:51:47Z"],["dc.date.available","2018-11-07T10:51:47Z"],["dc.date.issued","2004"],["dc.description.abstract","Histone macroH2A1.2 and the murine heterochromatin protein 1, HP1beta, have both been implicated in meiotic sex chromosome inactivation (MSCI) and the formation of the XY-body in male meiosis. In order to get a closer insight into the function of histone macroH2A1.2 we have investigated the localisation of macroH2A1.2 in surface spread spermatocytes from normal male mice and in oocytes of XX and XYTdym1 mice. Oocytes of XYTdym1 mice have no XY-body or MSCI despite having an XY chromosome constitution, so the presence or absence of 'XY-body' proteins in association with the X and/or Y chromosome of these oocytes enables some discrimination between potential functions of XY-body located proteins. We demonstrate here that macroH2A1.2 localises to the X and Y chromatin of spermatocytes as they condense to form the XY-body but is not associated with the X and Y chromatin of XYTdym1 early pachytene oocytes. MacroH2A1.2 and HP1beta co-localise to autosomal pericentromeric heterochromatin in spermatocytes. However, the two proteins show temporally and spatially distinct patterns of association to X and Y chromatin."],["dc.identifier.doi","10.1242/jcs.00851"],["dc.identifier.isi","000188665400007"],["dc.identifier.pmid","14676273"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48963"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0021-9533"],["dc.title","Localisation of histone macroH2A1.2 to the XY-body is not a response to the presence of asynapsed chromosome axes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2003Conference Abstract [["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell Motility and the Cytoskeleton"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Donkor, F. F."],["dc.contributor.author","Moennich, M."],["dc.contributor.author","Czirr, E."],["dc.contributor.author","Hoyer-Fender, Sigrid"],["dc.date.accessioned","2018-11-07T10:41:09Z"],["dc.date.available","2018-11-07T10:41:09Z"],["dc.date.issued","2003"],["dc.format.extent","178"],["dc.identifier.isi","000180795600073"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46467"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.publisher.place","New york"],["dc.relation.conference","EMBO/EMBL Conference on Centrosomes and Spindle Pole Bodies"],["dc.relation.eventlocation","HEIDELBERG, GERMANY"],["dc.relation.issn","0886-1544"],["dc.title","Interaction of the novel centrosomal protein ODF2 with cytoskeletal proteins"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS2004Journal Article [["dc.bibliographiccitation.firstpage","4643"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","4651"],["dc.bibliographiccitation.volume","117"],["dc.contributor.author","Donkor, F. F."],["dc.contributor.author","Monnich, M."],["dc.contributor.author","Czirr, E."],["dc.contributor.author","Hollemann, T."],["dc.contributor.author","Hoyer-Fender, Sigrid"],["dc.date.accessioned","2018-11-07T10:45:35Z"],["dc.date.available","2018-11-07T10:45:35Z"],["dc.date.issued","2004"],["dc.description.abstract","Outer dense fibre protein 2 (ODF2) is a major protein of sperm tail outer dense fibres which are prominent sperm tail-specific cytoskeletal structures. Moreover, ODF2 was also identified as a widespread component of the centrosomal scaffold and was found to associate preferentially with the appendages of the mother centriole [Nakagawa, Y., Yamane, Y., Okanoue, T., Tsukita, S. and Tsukita, S. (2001) Mol. Biol. Cell 12,1687-1.697]. Secondary structure predictions indicated ODF2 as an overall coiled-coil protein with a putative fibre forming capacity. To investigate its potential functions in generating the centrosomal scaffold and in microtubule nucleation we asked whether ODF2 is able to form a fibrillar structure by self-association in vivo and if it interacts with microtubules. By cytological investigation of transfected mammalian cells expressing ODF2-GFP fusion proteins and in vitro coprecipitation assays we could demonstrate that ODF2 is a self-interacting protein that forms a fibrillar structure partially linked to the microtubule network. Microtubule cosedimentation and coprecipitation assays indicated ODF2 as a microtubule-associated protein. However, we could not demonstrate a direct interaction of ODF2 with tubulin, suggesting that binding of endogenous ODF2 to the axonemal as well as to centrosomal microtubules may be mediated by, as yet, unknown proteins."],["dc.identifier.doi","10.1242/jcs.01303"],["dc.identifier.isi","000224718500006"],["dc.identifier.pmid","15340007"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/47533"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0021-9533"],["dc.title","Outer dense fibre protein 2 (ODF2) is a self-interacting centrosomal protein with affinity for microtubules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS