Publication Date:
2007-01-27
Description:
How do integral membrane proteins evolve in size and complexity? Using the small multidrug-resistance protein EmrE from Escherichia coli as a model, we experimentally demonstrated that the evolution of membrane proteins composed of two homologous but oppositely oriented domains can occur in a small number of steps: An original dual-topology protein evolves, through a gene-duplication event, to a heterodimer formed by two oppositely oriented monomers. This simple evolutionary pathway can explain the frequent occurrence of membrane proteins with an internal pseudo-two-fold symmetry axis in the plane of the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rapp, Mikaela -- Seppala, Susanna -- Granseth, Erik -- von Heijne, Gunnar -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1282-4. Epub 2007 Jan 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255477" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Antiporters/*chemistry/genetics
;
Cell Membrane/*chemistry
;
Dimerization
;
Directed Molecular Evolution
;
Drug Resistance, Bacterial
;
Escherichia coli/*chemistry/drug effects/genetics/growth & development
;
Escherichia coli Proteins/*chemistry/genetics
;
Ethidium/pharmacology
;
*Evolution, Molecular
;
Gene Duplication
;
Membrane Transport Proteins/*chemistry/genetics
;
Molecular Sequence Data
;
Mutation
;
Protein Folding
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protein Subunits/chemistry
;
Recombinant Fusion Proteins/chemistry/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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