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A new subfamily of major intrinsic proteins in plants.

Johanson, Urban LU and Gustavsson, Sofia LU (2002) In Molecular Biology and Evolution 19(4). p.456-461
Abstract
The major intrinsic proteins (MIPs) form a large protein family of ancient origin and are found in bacteria, fungi, animals, and plants. MIPs act as channels in membranes to facilitate passive transport across the membrane. Some MIPs allow small polar molecules like glycerol or urea to pass through the membrane. However, the majority of MIPs are thought to be aquaporins (AQPs), i.e., they are specific for water transport. Plant MIPs can be subdivided into the plasma membrane intrinsic protein, tonoplast intrinsic protein, and NOD26-like intrinsic protein subfamilies. By database mining and phylogenetic analyses, we have identified a new subfamily in plants, the Small basic Intrinsic Proteins (SIPs). Comparisons of sequences from the new... (More)
The major intrinsic proteins (MIPs) form a large protein family of ancient origin and are found in bacteria, fungi, animals, and plants. MIPs act as channels in membranes to facilitate passive transport across the membrane. Some MIPs allow small polar molecules like glycerol or urea to pass through the membrane. However, the majority of MIPs are thought to be aquaporins (AQPs), i.e., they are specific for water transport. Plant MIPs can be subdivided into the plasma membrane intrinsic protein, tonoplast intrinsic protein, and NOD26-like intrinsic protein subfamilies. By database mining and phylogenetic analyses, we have identified a new subfamily in plants, the Small basic Intrinsic Proteins (SIPs). Comparisons of sequences from the new subfamily with conserved amino acid residues in other MIPs reveal characteristic features of SIPs. Possible functional consequences of these features are discussed in relation to the recently solved structures of AQP1 and GlpF. We suggest that substitutions at conserved and structurally important positions imply a different substrate specificity for the new subfamily. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Algorithms, Amino Acid Sequence, Comparative Study, Expressed Sequence Tags, Gene Expression Profiling, Genes, Plant, Ion Channels : genetics, Molecular Sequence Data, Phylogeny, Species Specificity, Amino Acid, Sequence Homology, Plant Proteins : genetics
in
Molecular Biology and Evolution
volume
19
issue
4
pages
456 - 461
publisher
Oxford University Press
external identifiers
  • wos:000174967000010
  • pmid:11919287
  • scopus:0036221680
ISSN
0737-4038
language
English
LU publication?
yes
id
13d8ca16-d6ad-48e7-8786-819497561f5b (old id 107246)
alternative location
http://mbe.oxfordjournals.org/cgi/reprint/19/4/456
date added to LUP
2007-07-05 13:21:27
date last changed
2017-05-21 03:45:34
@article{13d8ca16-d6ad-48e7-8786-819497561f5b,
  abstract     = {The major intrinsic proteins (MIPs) form a large protein family of ancient origin and are found in bacteria, fungi, animals, and plants. MIPs act as channels in membranes to facilitate passive transport across the membrane. Some MIPs allow small polar molecules like glycerol or urea to pass through the membrane. However, the majority of MIPs are thought to be aquaporins (AQPs), i.e., they are specific for water transport. Plant MIPs can be subdivided into the plasma membrane intrinsic protein, tonoplast intrinsic protein, and NOD26-like intrinsic protein subfamilies. By database mining and phylogenetic analyses, we have identified a new subfamily in plants, the Small basic Intrinsic Proteins (SIPs). Comparisons of sequences from the new subfamily with conserved amino acid residues in other MIPs reveal characteristic features of SIPs. Possible functional consequences of these features are discussed in relation to the recently solved structures of AQP1 and GlpF. We suggest that substitutions at conserved and structurally important positions imply a different substrate specificity for the new subfamily.},
  author       = {Johanson, Urban and Gustavsson, Sofia},
  issn         = {0737-4038},
  keyword      = {Algorithms,Amino Acid Sequence,Comparative Study,Expressed Sequence Tags,Gene Expression Profiling,Genes,Plant,Ion Channels : genetics,Molecular Sequence Data,Phylogeny,Species Specificity,Amino Acid,Sequence Homology,Plant Proteins : genetics},
  language     = {eng},
  number       = {4},
  pages        = {456--461},
  publisher    = {Oxford University Press},
  series       = {Molecular Biology and Evolution},
  title        = {A new subfamily of major intrinsic proteins in plants.},
  volume       = {19},
  year         = {2002},
}