Change search
ReferencesLink to record
Permanent link

Direct link
Binding specificities of the GYF domains from two Saccharomyces cerevisiae Paralogs
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2007 (English)In: Protein Engineering, Design & Selection, Vol. 20, no 9, 443-52 p.Article in journal (Refereed) Published
Abstract [en]

We have used multivariate statistics and z-scales to represent peptide sequences in a PLS-QSAR model of previously studied binding affinities [ Kofler,M., Motzny,K. and Freund,C. (2005b) Mol. Cell. Proteomics, 4, 1797–1811.] of two GYF domains to an array of immobilized synthetic peptides. As a result, we established structural determinants of the binding specificities of the two proteins. Our model was used to define new sets of yeast proteins potentially interacting with Syh1 (YPL105C) and Smy2 (YBR172C). These sets were subsequently examined for co-occurrence of Gene Ontology terms, leading to suggest a group of likely interacting proteins with a common function in mRNA catabolism. Finally, subcellular localization of a GFP-fused Syh1 and Smy2 reinforced the possibility that these proteins reside in cytoplasmic sites of mRNA degradation, thereby providing experimental confirmation to the predictions from the model.

Place, publisher, year, edition, pages
2007. Vol. 20, no 9, 443-52 p.
Keyword [en]
URN: urn:nbn:se:umu:diva-16446DOI: 10.1093/protein/gzm041OAI: diva2:156119
Available from: 2008-05-30 Created: 2008-05-30 Last updated: 2013-03-19Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Sjöström, Michael
By organisation
Department of Chemistry

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 28 hits
ReferencesLink to record
Permanent link

Direct link