The fasciclin-like arabinogalactan proteins of arabidopsis. A multigene family of putative cell adhesion molecules

被引:298
作者
Johnson, KL
Jones, BJ
Bacic, A
Schultz, CJ
机构
[1] Univ Adelaide, Sch Agr & Wine, Glen Osmond, SA 5064, Australia
[2] Univ Melbourne, Sch Bot, Plant Cell Biol Ctr, Melbourne, Vic 3010, Australia
关键词
D O I
10.1104/pp.103.031237
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Fasciclin-like arabinogalactan proteins (FLAs) are a subclass of arabinogalactan proteins (AGPs) that have, in addition to predicted AGP-like glycosylated regions, putative cell adhesion domains known as fasciclin domains. In other eukaryotes (e.g. fruitfly [Drosophila melanogaster] and humans [Homo sapiens]), fasciclin domain-containing proteins are involved in cell adhesion. There are at least 21 FLAs in the annotated Arabidopsis genome. Despite the deduced proteins having low overall similarity, sequence analysis of the fasciclin domains in Arabidopsis FLAs identified two highly conserved regions that define this motif, suggesting that the cell adhesion function is conserved. We show that FLAs precipitate with beta-glucosyl Yariv reagent, indicating that they share structural characteristics with AGPs. Fourteen of the FLA family members are predicted to be C-terminally substituted with a glycosylphosphatidylinositol anchor, a cleavable form of membrane anchor for proteins, indicating different FLAs may have different developmental roles. Publicly available microarray and expressed sequence tag data were used to select FLAs for further expression analysis. RNA gel blots for a number of FLAs indicate that they are likely to be important during plant development and in response to abiotic stress. FLAs 1,2, and 8 show a rapid decrease in mRNA abundance in response to the phytohormone abscisic acid. Also, the accumulation of FLA1 and FLA2 transcripts differs during callus and shoot development, indicating that the proteins may be significant in the process of competence acquisition and induction of shoot development.
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页码:1911 / 1925
页数:15
相关论文
共 79 条
[31]   Glycosyl-phosphatidylinositol anchored membrane enzymes [J].
Hooper, NM .
CLINICA CHIMICA ACTA, 1997, 266 (01) :3-12
[32]  
HORTSCH M, 1990, J BIOL CHEM, V265, P15104
[33]  
Hu S, 1998, J NEUROBIOL, V35, P77, DOI 10.1002/(SICI)1097-4695(199804)35:1<77::AID-NEU7>3.0.CO
[34]  
2-8
[35]   ALGAL-CAMS - ISOFORMS OF A CELL-ADHESION MOLECULE IN EMBRYOS OF THE ALGA VOLVOX WITH HOMOLOGY TO DROSOPHILA FASCICLIN-I [J].
HUBER, O ;
SUMPER, M .
EMBO JOURNAL, 1994, 13 (18) :4212-4222
[36]   Analysis of the genome sequence of the flowering plant Arabidopsis thaliana [J].
Kaul, S ;
Koo, HL ;
Jenkins, J ;
Rizzo, M ;
Rooney, T ;
Tallon, LJ ;
Feldblyum, T ;
Nierman, W ;
Benito, MI ;
Lin, XY ;
Town, CD ;
Venter, JC ;
Fraser, CM ;
Tabata, S ;
Nakamura, Y ;
Kaneko, T ;
Sato, S ;
Asamizu, E ;
Kato, T ;
Kotani, H ;
Sasamoto, S ;
Ecker, JR ;
Theologis, A ;
Federspiel, NA ;
Palm, CJ ;
Osborne, BI ;
Shinn, P ;
Conway, AB ;
Vysotskaia, VS ;
Dewar, K ;
Conn, L ;
Lenz, CA ;
Kim, CJ ;
Hansen, NF ;
Liu, SX ;
Buehler, E ;
Altafi, H ;
Sakano, H ;
Dunn, P ;
Lam, B ;
Pham, PK ;
Chao, Q ;
Nguyen, M ;
Yu, GX ;
Chen, HM ;
Southwick, A ;
Lee, JM ;
Miranda, M ;
Toriumi, MJ ;
Davis, RW .
NATURE, 2000, 408 (6814) :796-815
[37]   Structural and phylogenetic analyses of RGD-CAP/βig-h3, a fasciclin-like adhesion protein expressed in chick chondrocytes [J].
Kawamoto, T ;
Noshiro, M ;
Shen, M ;
Nakamasu, K ;
Hashimoto, K ;
Kawashima-Ohya, Y ;
Gotoh, O ;
Kato, Y .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 1998, 1395 (03) :288-292
[38]   TANDEM MASS-SPECTROMETRY AND STRUCTURAL ELUCIDATION OF GLYCOPEPTIDES FROM A HYDROXYPROLINE-RICH PLANT-CELL WALL GLYCOPROTEIN INDICATE THAT CONTIGUOUS HYDROXYPROLINE RESIDUES ARE THE MAJOR SITES OF HYDROXYPROLINE O-ARABINOSYLATION [J].
KIELISZEWSKI, MJ ;
ONEILL, M ;
LEYKAM, J ;
ORLANDO, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (06) :2541-2549
[39]   EXTENSIN - REPETITIVE MOTIFS, FUNCTIONAL SITES, POSTTRANSLATIONAL CODES, AND PHYLOGENY [J].
KIELISZEWSKI, MJ ;
LAMPORT, DTA .
PLANT JOURNAL, 1994, 5 (02) :157-172
[40]   Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-β-induced gene, βig-h3 [J].
Kim, JE ;
Kim, SJ ;
Lee, BH ;
Park, RW ;
Kim, KS ;
Kim, IS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (40) :30907-30915