A novel plant major intrinsic protein in Physcomitrella patens most similar to bacterial glycerol channels
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/152465
- author
- Gustavsson, Sofia LU ; Lebrun, Anne-Sophie ; Nordén, Kristina LU ; Chaumont, François and Johanson, Urban LU
- organization
- publishing date
- 2005
- 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
- 2016-04-01 12:12:50
- date last changed
- 2022-03-28 21:51:19
@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}}, doi = {{10.1104/pp.105.063198}}, volume = {{139}}, year = {{2005}}, }