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MILDEW RESISTANCE LOCUS O Function in Pollen Tube Reception Is Linked to Its Oligomerization and Subcellular Distribution.
Jones, Daniel S; Yuan, Jing; Smith, Benjamin E; Willoughby, Andrew C; Kumimoto, Emily L; Kessler, Sharon A.
Affiliation
  • Jones DS; Department of Microbiology and Plant Biology, University of Oklahoma, Norman, Oklahoma 73069.
  • Yuan J; Department of Microbiology and Plant Biology, University of Oklahoma, Norman, Oklahoma 73069.
  • Smith BE; Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907.
  • Willoughby AC; Department of Microbiology and Plant Biology, University of Oklahoma, Norman, Oklahoma 73069.
  • Kumimoto EL; Vision Science, University of California, Berkeley, California 94720.
  • Kessler SA; Department of Microbiology and Plant Biology, University of Oklahoma, Norman, Oklahoma 73069.
Plant Physiol ; 175(1): 172-185, 2017 Sep.
Article in En | MEDLINE | ID: mdl-28724621
Sexual reproduction in flowering plants requires communication between synergid cells and a tip-elongating pollen tube (PT) for the successful delivery of sperm cells to the embryo sac. The reception of the PT relies on signaling within the synergid cell that ultimately leads to the degeneration of the receptive synergid and PT rupture, releasing the sperm cells for double fertilization. In Arabidopsis (Arabidopsis thaliana), NORTIA, a member of the MILDEW RESISTANCE LOCUS O (MLO) family of proteins, plays a critical role in the communication processes regulating PT reception. In this study, we determined that MLO function in PT reception is dependent on MLO protein localization into a Golgi-associated compartment before PT arrival, indicating that PT-triggered regulation of the synergid secretory system is important for synergid function during pollination. Additionally, a structure-function analysis revealed that MLO homooligomerization, mediated by the amino-terminal region of the protein, and carboxyl-terminal tail identity both contribute to MLO activity during PT reception.
Subject(s)

Full text: 1 Database: MEDLINE Main subject: Calmodulin-Binding Proteins / Arabidopsis / Arabidopsis Proteins / Pollen Tube / Ovule Language: En Journal: Plant Physiol Year: 2017 Type: Article

Full text: 1 Database: MEDLINE Main subject: Calmodulin-Binding Proteins / Arabidopsis / Arabidopsis Proteins / Pollen Tube / Ovule Language: En Journal: Plant Physiol Year: 2017 Type: Article