A fasciclin-like arabinogalactan-protein (FLA) mutant of Arabidopsis thaliana, fla1, shows defects in shoot regeneration

The fasciclin-like arabinogalactan-proteins (FLAs) are an enigmatic class of 21 members within the larger family of arabinogalactan-proteins (AGPs) in Arabidopsis thaliana. Located at the cell surface, in the cell wall/plasma membrane, they are implicated in many developmental roles yet their functi...

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Veröffentlicht in:PloS one 2011-09, Vol.6 (9), p.e25154-e25154
Hauptverfasser: Johnson, Kim L, Kibble, Natalie A J, Bacic, Antony, Schultz, Carolyn J
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Bacic, Antony
Schultz, Carolyn J
description The fasciclin-like arabinogalactan-proteins (FLAs) are an enigmatic class of 21 members within the larger family of arabinogalactan-proteins (AGPs) in Arabidopsis thaliana. Located at the cell surface, in the cell wall/plasma membrane, they are implicated in many developmental roles yet their function remains largely undefined. Fasciclin (FAS) domains are putative cell-adhesion domains found in extracellular matrix proteins of organisms from all kingdoms, but the juxtaposition of FAS domains with highly glycosylated AGP domains is unique to plants. Recent studies have started to elucidate the role of FLAs in Arabidopsis development. FLAs containing a single FAS domain are important for the integrity and elasticity of the plant cell wall matrix (FLA11 and FLA12) and FLA3 is involved in microspore development. FLA4/SOS5 with two FAS domains and two AGP domains has a role in maintaining proper cell expansion under salt stressed conditions. The role of other FLAs remains to be uncovered. Here we describe the characterisation of a T-DNA insertion mutant in the FLA1 gene (At5g55730). Under standard growth conditions fla1-1 mutants have no obvious phenotype. Based on gene expression studies, a putative role for FLA1 in callus induction was investigated and revealed that fla1-1 has a reduced ability to regenerate shoots in an in vitro shoot-induction assay. Analysis of FLA1p:GUS reporter lines show that FLA1 is expressed in several tissues including stomata, trichomes, the vasculature of leaves, the primary root tip and in lateral roots near the junction of the primary root. The results of the developmental expression of FLA1 and characterisation of the fla1 mutant support a role for FLA1 in the early events of lateral root development and shoot development in tissue culture, prior to cell-type specification.
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Located at the cell surface, in the cell wall/plasma membrane, they are implicated in many developmental roles yet their function remains largely undefined. Fasciclin (FAS) domains are putative cell-adhesion domains found in extracellular matrix proteins of organisms from all kingdoms, but the juxtaposition of FAS domains with highly glycosylated AGP domains is unique to plants. Recent studies have started to elucidate the role of FLAs in Arabidopsis development. FLAs containing a single FAS domain are important for the integrity and elasticity of the plant cell wall matrix (FLA11 and FLA12) and FLA3 is involved in microspore development. FLA4/SOS5 with two FAS domains and two AGP domains has a role in maintaining proper cell expansion under salt stressed conditions. The role of other FLAs remains to be uncovered. Here we describe the characterisation of a T-DNA insertion mutant in the FLA1 gene (At5g55730). Under standard growth conditions fla1-1 mutants have no obvious phenotype. Based on gene expression studies, a putative role for FLA1 in callus induction was investigated and revealed that fla1-1 has a reduced ability to regenerate shoots in an in vitro shoot-induction assay. Analysis of FLA1p:GUS reporter lines show that FLA1 is expressed in several tissues including stomata, trichomes, the vasculature of leaves, the primary root tip and in lateral roots near the junction of the primary root. The results of the developmental expression of FLA1 and characterisation of the fla1 mutant support a role for FLA1 in the early events of lateral root development and shoot development in tissue culture, prior to cell-type specification.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21966441</pmid><doi>10.1371/journal.pone.0025154</doi><oa>free_for_read</oa></addata></record>
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subjects Analysis
Arabidopsis
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis - physiology
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Arabidopsis thaliana
Arabinogalactan
Biology
Callus
Cell adhesion & migration
Cell culture
Cell surface
Cell walls
Deoxyribonucleic acid
DNA
Elasticity
Extracellular matrix
Gene expression
Glycoproteins
Growth conditions
Kinases
Leaves
Microscopy
Mucoproteins - genetics
Mucoproteins - metabolism
Mutants
Plant Proteins - genetics
Plant Proteins - metabolism
Plant Shoots - genetics
Plant Shoots - metabolism
Plant Shoots - physiology
Proteins
Rape plants
Regeneration
Root development
Salts
Shoots
Stomata
Studies
T-DNA
Tissue culture
Tissues
Trichomes
title A fasciclin-like arabinogalactan-protein (FLA) mutant of Arabidopsis thaliana, fla1, shows defects in shoot regeneration
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T06%3A05%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20fasciclin-like%20arabinogalactan-protein%20(FLA)%20mutant%20of%20Arabidopsis%20thaliana,%20fla1,%20shows%20defects%20in%20shoot%20regeneration&rft.jtitle=PloS%20one&rft.au=Johnson,%20Kim%20L&rft.date=2011-09-22&rft.volume=6&rft.issue=9&rft.spage=e25154&rft.epage=e25154&rft.pages=e25154-e25154&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0025154&rft_dat=%3Cgale_plos_%3EA476877987%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1308524492&rft_id=info:pmid/21966441&rft_galeid=A476877987&rft_doaj_id=oai_doaj_org_article_2db5112c64504e9a8f125eccfcc7fffa&rfr_iscdi=true