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Functional Dissection of the Drosophila melanogaster Condensin Subunit Cap-G Reveals Its Exclusive Association with Condensin I

Title data

Herzog, Sabine ; Nagarkar-Jaiswal, Sonal ; Urban, Evelin ; Riemer, Anna ; Fischer, Sina ; Heidmann, Stefan:
Functional Dissection of the Drosophila melanogaster Condensin Subunit Cap-G Reveals Its Exclusive Association with Condensin I.
In: PLoS Genetics. Vol. 9 (2013) Issue 4 . - e1003463.
ISSN 1553-7404
DOI: https://doi.org/10.1371/journal.pgen.1003463

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Abstract in another language

The heteropentameric condensin complexes have been shown to participate in mitotic chromosome condensation and to be required for unperturbed chromatid segregation in nuclear divisions. Vertebrates have two condensin complexes, condensin I and condensin II, which contain the same structural maintenance of chromosomes (SMC) subunits SMC2 and SMC4, but differ in their composition of non-SMC subunits. While a clear biochemical and functional distinction between condensin I and condensin II has been established in vertebrates, the situation in Drosophila melanogaster is less defined. Since Drosophila lacks a clear homolog for the condensin II-specific subunit Cap-G2, the condensin I subunit Cap-G has been hypothesized to be part of both complexes. In vivo microscopy revealed that a functional Cap-G-EGFP variant shows a distinct nuclear enrichment during interphase, which is reminiscent of condensin II localization in vertebrates and contrasts with the cytoplasmic enrichment observed for the other EGFP-fused condensin I subunits. However, we show that this nuclear localization is dispensable for Cap-G chromatin association, for its assembly into the condensin I complex and, importantly, for development into a viable and fertile adult animal. Immunoprecipitation analyses and complex formation studies provide evidence that Cap-G does not associate with condensin II-specific subunits, while it can be readily detected in complexes with condensin I-specific proteins in vitro and in vivo. Mass-spectrometric analyses of proteins associated with the condensin II-specific subunit Cap-H2 not only fail to identify Cap-G but also the other known condensin II-specific homolog Cap-D3. As condensin II-specific subunits are also not found associated with SMC2, our results question the existence of a soluble condensin II complex in Drosophila.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Drosophila melanogaster; Chromatin; Immunoprecipitation; condensin complexes; Mitosis; Mitotic chromosome condensation; Gene-expression; Sister chromatids; Protein; Complex; Heterochromatin; Interphase; Mitosis; Cells; Identification
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Genetics
Research Institutions
Result of work at the UBT: Yes
DDC Subjects: 500 Science
500 Science > 570 Life sciences, biology
Date Deposited: 04 Jul 2015 21:00
Last Modified: 10 Mar 2020 12:13
URI: https://eref.uni-bayreuth.de/id/eprint/15786