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Review of 'Interactions between the transmembrane domains of CD39: identification of interacting residues by yeast selection.'

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4
The article is well written and the experimental plan is sound
Average rating:
    Rated 4 of 5.
Level of importance:
    Rated 3 of 5.
Level of validity:
    Rated 4 of 5.
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    Rated 4 of 5.
Level of comprehensibility:
    Rated 4 of 5.
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None

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Interactions between the transmembrane domains of CD39: identification of interacting residues by yeast selection.

 Guido Guidotti (corresponding) ,  Sari Paavilainen (2014)
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 domains.
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    Review information

    10.14293/S2199-1006.1.SOR-LIFE.AEEERM.v1.RBPTUK

    This work has been published open access under Creative Commons Attribution License CC BY 4.0, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Conditions, terms of use and publishing policy can be found at www.scienceopen.com.

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    Review text

    The article by Paavilainen and Guidotti deals with interaction of residues of vicinal transmembrane domains of CD 39. There are convincing experimental evidences, even though indirect, on the interactions identified.

    I would suggest to improve Fig. 4 which has an obsolete representation of residues. A tridimensional view of the alpha-helix structures should be shown. These can be obtained by modelling CD39 on a similar protein or, if not available, just by energy minimization on the single alpha-helices. Ribbon representation with the important residues highlighted would be optimal.

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