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Phylogenetic analyses and expression studies reveal two distinct groups of calreticulin isoforms in higher plants.

Persson, Staffan LU ; Rosenquist, Magnus LU ; Svensson, Karin; Galvao, R; Boss, W F and Sommarin, Marianne LU (2003) In Plant Physiology 133(3). p.1385-1396
Abstract
Calreticulin (CRT) is a multifunctional protein mainly localized to the endoplasmic reticulum in eukaryotic cells. Here, we present the first analysis, to our knowledge, of evolutionary diversity and expression profiling among different plant CRT isoforms. Phylogenetic studies and expression analysis show that higher plants contain two distinct groups of CRTs: a CRT1/CRT2 group and a CRT3 group. To corroborate the existence of these isoform groups, we cloned a putative CRT3 ortholog from Brassica rapa. The CRT3 gene appears to be most closely related to the ancestral CRT gene in higher plants. Distinct tissue-dependent expression patterns and stress-related regulation were observed for the isoform groups. Furthermore, analysis of... (More)
Calreticulin (CRT) is a multifunctional protein mainly localized to the endoplasmic reticulum in eukaryotic cells. Here, we present the first analysis, to our knowledge, of evolutionary diversity and expression profiling among different plant CRT isoforms. Phylogenetic studies and expression analysis show that higher plants contain two distinct groups of CRTs: a CRT1/CRT2 group and a CRT3 group. To corroborate the existence of these isoform groups, we cloned a putative CRT3 ortholog from Brassica rapa. The CRT3 gene appears to be most closely related to the ancestral CRT gene in higher plants. Distinct tissue-dependent expression patterns and stress-related regulation were observed for the isoform groups. Furthermore, analysis of posttranslational modifications revealed differences in the glycosylation status among members within the CRT1/CRT2 isoform group. Based on evolutionary relationship, a new nomenclature for plant CRTs is suggested. The presence of two distinct CRT isoform groups, with distinct expression patterns and posttranslational modifications, supports functional specificity among plant CRTs and could account for the multiple functional roles assigned to CRTs. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Plant Physiology
volume
133
issue
3
pages
1385 - 1396
publisher
American Society of Plant Biologists
external identifiers
  • wos:000186644600043
  • pmid:14563927
  • scopus:0344961215
ISSN
1532-2548
DOI
10.1104/pp.103.024943
language
English
LU publication?
yes
id
e21a1a03-2e56-4bc4-843f-ecd942152f38 (old id 132700)
date added to LUP
2007-07-06 13:15:44
date last changed
2018-02-04 03:21:43
@article{e21a1a03-2e56-4bc4-843f-ecd942152f38,
  abstract     = {Calreticulin (CRT) is a multifunctional protein mainly localized to the endoplasmic reticulum in eukaryotic cells. Here, we present the first analysis, to our knowledge, of evolutionary diversity and expression profiling among different plant CRT isoforms. Phylogenetic studies and expression analysis show that higher plants contain two distinct groups of CRTs: a CRT1/CRT2 group and a CRT3 group. To corroborate the existence of these isoform groups, we cloned a putative CRT3 ortholog from Brassica rapa. The CRT3 gene appears to be most closely related to the ancestral CRT gene in higher plants. Distinct tissue-dependent expression patterns and stress-related regulation were observed for the isoform groups. Furthermore, analysis of posttranslational modifications revealed differences in the glycosylation status among members within the CRT1/CRT2 isoform group. Based on evolutionary relationship, a new nomenclature for plant CRTs is suggested. The presence of two distinct CRT isoform groups, with distinct expression patterns and posttranslational modifications, supports functional specificity among plant CRTs and could account for the multiple functional roles assigned to CRTs.},
  author       = {Persson, Staffan and Rosenquist, Magnus and Svensson, Karin and Galvao, R and Boss, W F and Sommarin, Marianne},
  issn         = {1532-2548},
  language     = {eng},
  number       = {3},
  pages        = {1385--1396},
  publisher    = {American Society of Plant Biologists},
  series       = {Plant Physiology},
  title        = {Phylogenetic analyses and expression studies reveal two distinct groups of calreticulin isoforms in higher plants.},
  url          = {http://dx.doi.org/10.1104/pp.103.024943},
  volume       = {133},
  year         = {2003},
}