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A novel glycine-rich protein is associated with starch grain accumulation during anther development

LIM14, originally identified ass a lily gene associated with microsporogenesis, encodes a protein which has two distinct domains, one with glycine-serine repeats and the other with a hydrophobic signal peptide at the N-terminus. The putative LIM14 protein, however, is distinct from the glycine-rich...

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Bibliographic Details
Published in:Plant and cell physiology 1999-04, Vol.40 (4), p.406-416
Main Authors: Mousavi, A. (narakou), Hiratsuka, R, Takase, H, Hiratsuka, K, Hotta, Y
Format: Article
Language:English
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Summary:LIM14, originally identified ass a lily gene associated with microsporogenesis, encodes a protein which has two distinct domains, one with glycine-serine repeats and the other with a hydrophobic signal peptide at the N-terminus. The putative LIM14 protein, however, is distinct from the glycine-rich cell wall proteins which have been described before. RNA analyses indicated that the LIM14 transcript is specifically detected in the anther from zygotene to young pollen stage. By using antibodies raised against recombinant LIM14 protein, we detected anther-specific 15 kDa protein. Immunofluorescence microscopy demonstrated that the LIM14 protein is associated with starch grains in the anther wan cells just prior to microspore mitosis and then accumulates at a higher level with the starch grains of immature pollen. We tagged LIM14 with the GUS and GFP reporter genes and introduced them into tobacco BY-2 cells. Analysis of the transformed cells revealed that the chimeric proteins are functional and specifically targeted to plastids. These results indicate that LIM14 is an anther-specific protein that may play a role in starch accumulation and amyloplast differentiation during anther development and pollen formation
ISSN:0032-0781
1471-9053
DOI:10.1093/oxfordjournals.pcp.a029556