Characterization of the pollen specific protein P24 from Camellia japonica

DOI Web Site 25 References
  • USUKI Hiroyuki
    Graduate School of Integrated Science, Yokohama City University
  • YAJIMA Yuhki
    Graduate School of Integrated Science, Yokohama City University
  • MOGAMI Norifumi
    Graduate School of Integrated Science, Yokohama City University
  • TANAKA Kouhei
    Graduate School of Integrated Science, Yokohama City University
  • NAKAMURA Norio
    Graduate School of Integrated Science, Yokohama City University

Bibliographic Information

Other Title
  • ツバキ花粉特異的蛋白質P24の性質
  • ツバキ カフン トクイテキ タンパクシツ P24 ノ セイシツ

Search this article

Abstract

During a course of studies relating to the physiological functions of pollen-specific proteins, protein P24 was isolated from mature pollen grains of Camellia japonica. The protein is characterized by a molecular weigh of 23.5kDa and an isoelectric point (pI) of 5.4: a specific antiserum was raised against it. The pollen-specific P24, which has only been detected in pollen of the genus Camellia, was glycosylated. Subsequent incubation of the pollen grains deglycosylated P24 to generate P20 protein with a molecular mass of 20.3kDa and a pI of 5.4. The amino acid sequence of P24 deduced by cloning of the gene showed a very high homology with amino acid sequence of three other pollen-specific proteins: LAT52 from Tomato, Ole e I from Olive, and Zmc 13 from Maize. It has been reported that these pollen-specific proteins have functions that are closely related to pollen germination and tube growth. Furthermore, SPORT and SignalP analyses suggested that P24 is a secretory protein. Immunoelectron microscopy indicated that P24 in the cytosol is transferred to the intine and tube wall during pollen germination and tube growth. These results suggest that P24 protein has functions that are closely associated with pollen germination and tube growth.

Journal

References(25)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top