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Structure predictions and interaction studies indicate homology of separase N-terminal regulatory domains and Drosophila THR

Title data

Jager, H. ; Herzig, B. ; Herzig, A. ; Sticht, H. ; Lehner, Christian F. ; Heidmann, Stefan:
Structure predictions and interaction studies indicate homology of separase N-terminal regulatory domains and Drosophila THR.
In: Cell Cycle. Vol. 3 (2004) Issue 2 . - pp. 182-188.
ISSN 1551-4005

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Abstract in another language

The final resolution of sister chromatid cohesion during mitotic and meiotic divisions is mediated by activation of separase which cleaves a cohesin complex subunit. The structural basis of separase regulation is unknown. Separases from different eukaryotes share almost no sequence similarity, especially within the large N-terminal domain that precedes the protease domain except in Drosophila melanogaster. Moreover, sequence similarity among securin proteins, which associate as regulatory subunits with separase, is restricted to the signals that promote the mitotic degradation required for separase activation. Here, we address the surprising divergence of separase and securin sequences. The absence of an extended N-terminal separase domain in dipteran species is shown to be correlated with the expression of an extra regulatory subunit (THR). The interactions of THR with separase and securin in Drosophila melanogaster are analogous to those of the human N-terminal separase domain with its C-terminal domain and securin. Even heterologous interactions between Drosophila and human separase complex components occur in yeast two-hybrid experiments. Tertiary structure predictions reveal alpha-alpha superhelix folds in both THR and the N-terminal domains of nondipteran separases. The compatibility of these folds with a wide range of primary sequences has likely allowed the rapid divergence of THR/N-terminal separase sequences and securins, which contact this region

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: chromosome segregation; mitosis; meiosis; securin; separase; alpha-alpha superhelix;
protein-structure prediction; sister-chromatid separation; fold-recognition; promotes anaphase; evolution; cleavage; securin; program; repeats; binding
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Genetics
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 06 Mar 2020 11:07
Last Modified: 06 Mar 2020 11:07
URI: https://eref.uni-bayreuth.de/id/eprint/54535