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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ermolova, Natalia Kaback, H. Ronald Guan, Lan |
| Description | Author Affiliation: Ermolova N ( Howard Hughes Medical Institute, Department of Physiology and Microbiology, University of California, Los Angeles, CA 90095-1662, USA.); |
| Abstract | Previous experiments using intermolecular thiol cross-linking to determine surface-exposed positions in the transmembrane helices of the lactose permease suggest that only positions accessible from the aqueous phase are susceptible to cross-linking. This approach is now extended to most of the remaining positions in the molecule. Of an additional 143 single-Cys mutants studied, homodimer formation is observed with both a 5-A- and a 21-A-long crosslinking agent containing bis-methane thiosulfonate reactive groups in 33 mutants and exclusively with the 21-A-long reagent in 43 mutants. Furthermore, intermolecular cross-linking has little or no effect on transport activity, thereby providing further support for the argument that lactose permease is functionally, as well as structurally, a monomer in the membrane. In addition, evidence is presented indicating that reentrance loops are unlikely in this polytopic membrane transport protein. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 18 |
| Volume Number | 100 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2003-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Escherichia Coli Proteins Chemistry Escherichia Coli Enzymology Membrane Transport Proteins Monosaccharide Transport Proteins Sulfhydryl Compounds Symporters Amino Acid Sequence Biological Transport Lactose Metabolism Physiology Molecular Sequence Data Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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