These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Activity of protein MalE (maltose-binding protein) fused to cytoplasmic and periplasmic regions of an Escherichia coli inner membrane protein.
    Author: Dassa E, Lambert P.
    Journal: Res Microbiol; 1997 Jun; 148(5):389-95. PubMed ID: 9765817.
    Abstract:
    We analysed the properties of mature MBP (maltose-binding protein or MalE protein) fused to an integral cytoplasmic membrane protein of Escherichia coli. Fusion of MalE to the first MalG periplasmic loop enabled a strain defective in the malE gene to utilize maltose. In contrast, fusion of MalE to a cytoplasmic loop did not complement the malE delta 444 deletion. We obtained results highly correlated with those obtained by using alkaline phosphatase as a reporter for the topology of MalG. We discuss the possibility of genetically determining the topology of cytoplasmic membrane proteins by a method based on engineered fusions to MBP.
    [Abstract] [Full Text] [Related] [New Search]