Interactions between the transmembrane domains of CD39 : identification of interacting residues by yeast selection
View/ Open
Published Version
https://doi.org/10.14293/S2199-1006.1.SORLIFE.AEEERM.v1Metadata
Show full item recordCitation
Paavilainen, Sari and Guidotti, Guido. 2014. Interactions between the transmembrane domains of CD39: identification of interacting residues by yeast selection. ScienceOpen Research, 13 October 2014.Abstract
Rat CD39, a membrane-bound ectonucleoside triphosphate diphosphohydrolase that hydrolyzes extracellular nucleoside tri- and diphosphates, is anchored to the membrane by two transmembrane domains at the two ends of the molecule. The transmembrane domains are important for enzymatic activity, as mutants lacking one or both of these domains have a fraction of the enzymatic activity of the wild-type CD39. We investigated the interactions between the transmembrane domains by using a strain of yeast that requires surface expression of CD39 for growth. Random mutagenesis of selected amino acid residues in the N-terminal transmembrane domain revealed that the presence of charged amino acids at these positions prevents expression of functional protein. Rescue of the growth of these mutants by complementary mutations on selected residues of the C-terminal transmembrane domain indicates that there is contact between particular faces of the transmembrane domainsOther Sources
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4526264/Terms of Use
This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAACitable link to this page
http://nrs.harvard.edu/urn-3:HUL.InstRepos:23953012
Collections
- FAS Scholarly Articles [18292]
Contact administrator regarding this item (to report mistakes or request changes)