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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 experimental procedure is properly done and the analysis of the data is sound.
Average rating:
    Rated 4 of 5.
Level of importance:
    Rated 4 of 5.
Level of validity:
    Rated 4 of 5.
Level of completeness:
    Rated 4 of 5.
Level of comprehensibility:
    Rated 4 of 5.
Competing interests:
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.RYMFGI

    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

    Data are presented from yeast selection experiments to address inter-helical contact amino acids of the two transmembrane domains (TMDs) of CD39 relevant for the function of the protein. CD39 hydrolyzes nucleoside tri- and diphosphates and dynamics of the TMDs seem to be essential for enzymatic activity. Experimental results are transferred into helical wheal projections.

    The experimental procedure is properly done and the analysis of the data is sound.

    Some minor points:

    Page 5: second column, first paragraph: It is written about the findings using ΔTM1CD39 and referred to figure 2. But in this figure it is not obvious which curve relates to ΔTM1CD39. Making the naming consistent would help to read the manuscript.

    There is a large bit of very detailed discussion but the overall view is hard to grasp. It is e.g. hard to envision the mutations being done. A graph showing the TMDs as rods and indicating the mutations would be helpful to get a grasp of the idea behind the amino acids selected for mutation.

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