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A novel plant major intrinsic protein in Physcomitrella patens most similar to bacterial glycerol channels

Gustavsson, Sofia LU ; Lebrun, Anne-Sophie; Nordén, Kristina LU ; Chaumont, François and Johanson, Urban LU (2005) In Plant Physiology 139(1). p.287-295
Abstract
A gene encoding a novel fifth type of major intrinsic protein (MIP) in plants has been identified in the moss Physcomitrella patens. Phylogenetic analyses show that this protein, GlpF-like intrinsic protein (GIP1;1), is closely related to a subclass of glycerol transporters in bacteria that in addition to glycerol are highly permeable to water. A likely explanation of the occurrence of this bacterial-like MIP in P. patens is horizontal gene transfer. The expressed P. patens GIP1;1 gene contains five introns and encodes a unique C-loop extension of approximately 110 amino acid residues that has no obvious similarity with any other known protein. Based on alignments and structural comparisons with other MIPs, GIP1;1 is suggested to have... (More)
A gene encoding a novel fifth type of major intrinsic protein (MIP) in plants has been identified in the moss Physcomitrella patens. Phylogenetic analyses show that this protein, GlpF-like intrinsic protein (GIP1;1), is closely related to a subclass of glycerol transporters in bacteria that in addition to glycerol are highly permeable to water. A likely explanation of the occurrence of this bacterial-like MIP in P. patens is horizontal gene transfer. The expressed P. patens GIP1;1 gene contains five introns and encodes a unique C-loop extension of approximately 110 amino acid residues that has no obvious similarity with any other known protein. Based on alignments and structural comparisons with other MIPs, GIP1;1 is suggested to have retained the permeability for glycerol but not for water. Studies on heterologously expressed GIP1;1 in Xenopus laevis oocytes confirm the predicted substrate specificity. Interestingly, proteins of one of the plant-specific subgroups of MIPs, the NOD26-like intrinsic proteins, are also facilitating the transport of glycerol and have previously been suggested to have evolved from a horizontally transferred bacterial gene. Further studies on localization and searches for GIP1;1 homologs in other plants will clarify the function and significance of this new plant MIP. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Plant Physiology
volume
139
issue
1
pages
287 - 295
publisher
American Society of Plant Biologists
external identifiers
  • pmid:16113222
  • wos:000231765300027
  • scopus:33644808731
ISSN
1532-2548
DOI
10.1104/pp.105.063198
language
English
LU publication?
yes
id
86694f7b-e8bb-4ecf-8eb0-ecf2daa8b84c (old id 152465)
date added to LUP
2007-07-05 10:57:28
date last changed
2017-07-09 03:41:22
@article{86694f7b-e8bb-4ecf-8eb0-ecf2daa8b84c,
  abstract     = {A gene encoding a novel fifth type of major intrinsic protein (MIP) in plants has been identified in the moss Physcomitrella patens. Phylogenetic analyses show that this protein, GlpF-like intrinsic protein (GIP1;1), is closely related to a subclass of glycerol transporters in bacteria that in addition to glycerol are highly permeable to water. A likely explanation of the occurrence of this bacterial-like MIP in P. patens is horizontal gene transfer. The expressed P. patens GIP1;1 gene contains five introns and encodes a unique C-loop extension of approximately 110 amino acid residues that has no obvious similarity with any other known protein. Based on alignments and structural comparisons with other MIPs, GIP1;1 is suggested to have retained the permeability for glycerol but not for water. Studies on heterologously expressed GIP1;1 in Xenopus laevis oocytes confirm the predicted substrate specificity. Interestingly, proteins of one of the plant-specific subgroups of MIPs, the NOD26-like intrinsic proteins, are also facilitating the transport of glycerol and have previously been suggested to have evolved from a horizontally transferred bacterial gene. Further studies on localization and searches for GIP1;1 homologs in other plants will clarify the function and significance of this new plant MIP.},
  author       = {Gustavsson, Sofia and Lebrun, Anne-Sophie and Nordén, Kristina and Chaumont,  François  and Johanson, Urban},
  issn         = {1532-2548},
  language     = {eng},
  number       = {1},
  pages        = {287--295},
  publisher    = {American Society of Plant Biologists},
  series       = {Plant Physiology},
  title        = {A novel plant major intrinsic protein in Physcomitrella patens most similar to bacterial glycerol channels},
  url          = {http://dx.doi.org/10.1104/pp.105.063198},
  volume       = {139},
  year         = {2005},
}