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Internal duplications in alpha-helical membrane protein topologies are common but the nonduplicated forms are rare

Hennerdal, Aron (author)
Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
Falk, Jenny (author)
Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
Lindahl, Erik (author)
Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
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Elofsson, Arne (author)
Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
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 (creator_code:org_t)
2010-11-18
2010
English.
In: Protein Science. - : Wiley. - 0961-8368 .- 1469-896X. ; 19:12, s. 2305-2318
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Many alpha-helical membrane proteins contain internal symmetries, indicating that they might have evolved through a gene duplication and fusion event Here, we have characterized internal duplications among membrane proteins of known structure and in three complete genomes We found that the majority of large transmembrane (TM) proteins contain an internal duplication The duplications found showed a large variability both in the number of TM-segments included and in their orientation Surprisingly, an approximately equal number of antiparallel duplications and parallel duplications were found However, of all 11 superfamilies with an internal duplication, only for one, the AcrB Multidrug Efflux Pump, the duplicated unit could be found in its nonduplicated form An evolutionary analysis of the AcrB homologs indicates that several independent fusions have occurred, including the fusion of the SecD and SecF proteins into the 12-TM-protein SecDF in Brucella and Staphylococcus aureus In one additional case, the Vitamin B-12 transporter-like ABC transporters, the protein had undergone an additional fusion to form protein with 20 TM-helices in several bacterial genomes Finally, homologs to all human membrane proteins were used to detect the presence of duplicated and nonduplicated proteins This confirmed that only in rare cases can homologs with different duplication status be found, although internal symmetry is frequent among these proteins One possible explanation is that it is frequent that duplication and fusion events happen simultaneously and that there is almost always a strong selective advantage for the fused form

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)

Keyword

membrane proteins
gene duplication
protein evolution
gene fusion
Biochemistry
Biokemi
Molecular biology
Molekylärbiologi
Biochemistry
biokemi
Molecular Biology
molekylärbiologi

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ref (subject category)
art (subject category)

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