Abstract:
:Membrane proteins must balance the sequence constraints associated with folding and function against the hydrophobicity required for solvation within the bilayer. We recently found the expression and maturation of rhodopsin are limited by the hydrophobicity of its seventh transmembrane domain (TM7), which contains polar residues that are essential for function. On the basis of these observations, we hypothesized that rhodopsin's expression should be less tolerant of mutations in TM7 relative to those within hydrophobic TM domains. To test this hypothesis, we used deep mutational scanning to compare the effects of 808 missense mutations on the plasma membrane expression of rhodopsin in HEK293T cells. Our results confirm that a higher proportion of mutations within TM7 (37%) decrease rhodopsin's plasma membrane expression relative to those within a hydrophobic TM domain (TM2, 25%). These results in conjunction with an evolutionary analysis suggest solvation energetics likely restricts the evolutionary sequence space of polar TM domains.
journal_name
Sci Advjournal_title
Science advancesauthors
Penn WD,McKee AG,Kuntz CP,Woods H,Nash V,Gruenhagen TC,Roushar FJ,Chandak M,Hemmerich C,Rusch DB,Meiler J,Schlebach JPdoi
10.1126/sciadv.aay7505subject
Has Abstractpub_date
2020-03-04 00:00:00pages
eaay7505issue
10issn
2375-2548pii
aay7505journal_volume
6pub_type
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