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Possible link between a 35 kDa membrane protein and osmolyte transport in Staphylococcus aureus
Author(s) -
Pourkomailian
Publication year - 1998
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.1998.00306.x
Subject(s) - osmolyte , betaine , staphylococcus aureus , membrane transport , membrane protein , mutant , membrane transport protein , transposable element , transport protein , glycine , biochemistry , chemistry , biology , membrane , bacteria , amino acid , genetics , gene
Accumulation of proline and glycine betaine occurs via three transport systems in Staphylococcus aureus (Pourkomailian and Booth 1992, 1994). A 35 kDa membrane protein was identified to be missing from a mutant, BP108, which lacks activity of the low affinity osmolyte transport system. The loss in activity of the low affinity transport system may be linked to the loss in expression of the 35 kDa membrane protein as a result of transposon insertion.