Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling
- Max Planck Institute of Molecular Physiology, Germany
- IFOM—The FIRC Institute of Molecular Oncology, Italy
- University Duisburg-Essen, Germany
Peer review process
This article was accepted for publication as part of eLife's original publishing model.
History
- Version of Record published
- Accepted
- Received
Decision letter
-
Jon PinesReviewing Editor; The Gurdon Institute, United Kingdom
eLife posts the editorial decision letter and author response on a selection of the published articles (subject to the approval of the authors). An edited version of the letter sent to the authors after peer review is shown, indicating the substantive concerns or comments; minor concerns are not usually shown. Reviewers have the opportunity to discuss the decision before the letter is sent (see review process). Similarly, the author response typically shows only responses to the major concerns raised by the reviewers.
Thank you for submitting your work entitled “Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling” for consideration at eLife. Your article has been favorably evaluated by a Senior editor and three reviewers, one of whom is a member of the Board of Reviewing Editors.
One referee would like you to perform the following experiments to support your conclusions:
1) Arg239 that contacts pThr is a Lys in most Bub1 orthologs. Did the authors test whether a Lys substitution can still bind MELT peptides?
2) The authors suggest that Arg314 mediates the Bub1-dependent increased affinity of Bub3 for MELT peptides. What happens to the Bub1-mediated increase in binding when Arg314 is mutated?
https://doi.org/10.7554/eLife.01030.023Author response
1) Arg239 that contacts pThr is a Lys in most Bub1 orthologs. Did the authors test whether a Lys substitution can still bind MELT peptides?
[Editors' note: at the authors' request, the answer to this question has not been published to avoid disclosing confidential information.]
2) The authors suggest that Arg314 mediates the Bub1-dependent increased affinity of Bub3 for MELT peptides. What happens to the Bub1-mediated increase in binding when Arg314 is mutated?
This was an interesting suggestion. We have carried out an additional calorimetry experiment with the Bub1R314A mutant. In agreement with the hypothesis that this residue contributes to recognition of the phosphorylated MELT peptide, we find that the R314A mutant binds the MELT2P peptide with ∼3- to 4-fold reduced affinity. We have included the new ITC data as Figure 4F.
https://doi.org/10.7554/eLife.01030.024Download links
A two-part list of links to download the article, or parts of the article, in various formats.
Downloads (link to download the article as PDF)
Open citations (links to open the citations from this article in various online reference manager services)
Cite this article (links to download the citations from this article in formats compatible with various reference manager tools)
Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling
eLife 2:e01030.
https://doi.org/10.7554/eLife.01030
