4.7 Article

Acquisition of LURE-Binding Activity at the Pollen Tube Tip of Torenia fournieri

期刊

MOLECULAR PLANT
卷 6, 期 4, 页码 1074-1090

出版社

CELL PRESS
DOI: 10.1093/mp/sst050

关键词

pollen tube guidance; attractants; pollen tube; de novo transcriptome; proteome

资金

  1. Japan Society for the Promotion of Science [22005954, 23012021, 24113510, 24570045]
  2. Ministry of Education, Culture, Sports, Science and Technology of Japan [18075004, 19370017]
  3. Japan Science and Technology Agency (PRESTO)
  4. Japan Science and Technology Agency (ERATO project)
  5. Yamada Science Foundation
  6. Mitsubishi Foundation

向作者/读者索取更多资源

We show that, in the pollen tube guidance of Torenia, binding of an attractant peptide LURE at the tube tip and response competency to LURE are differently controlled by the pistil tissue. Transcriptome and proteome data of pollen tubes are also provided.Pollen tube guidance is controlled by multiple complex interactions with the female tissues. Here, we show that pollen tubes of Torenia fournieri are regulated by a stylar tissue in a length-dependent manner to receive and respond to attractant LURE peptides secreted from synergid cells. We developed an immunostaining method to visualize LURE peptides bound at the plasma membrane of the tip region of the pollen tube. Using this method, we found that LURE peptides bound specifically to pollen tubes growing through a cut style. The peptides also bound to pollen tubes growing through a shorter style, which were not competent to respond to these peptides. These observations suggested a possibility that acquisition of the LURE peptide reception ability and acquisition of full competency are separable processes. RNA-Seq suggested that the transcription profile of pollen tubes was affected by both the length of the style and the cultivation period, consistently with physiological changes in binding activity and LURE response ability. The database generated from de novo RNA-Seq of Torenia pollen tubes was shown to be useful to identify pollen tube proteins by mass spectrometry. Our studies provide insight and an effective platform for protein identification to understand pollen tube guidance.

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