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Related Experiment Videos

Pollen profilin function depends on interaction with proline-rich motifs

B C Gibbon1, L E Zonia, D R Kovar

  • 1Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.

The Plant Cell
|June 23, 1998
PubMed
Summary

New maize profilin ZmPRO4, predominantly in endosperm, shows higher poly-L-proline binding. This profilin isoform impacts actin cytoskeletal dynamics and nuclear positioning in plant cells more rapidly than other isoforms.

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Area of Science:

  • Plant Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Profilins are actin-binding proteins crucial for regulating actin polymerization in vitro and in vivo.
  • Plants possess diverse profilin gene families, leading to multiple profilin isoforms with potentially distinct functions.
  • Previous studies characterized maize pollen profilins for their effects on plant cell cytoarchitecture and interactions with actin and poly-L-proline.

Purpose of the Study:

  • To characterize a novel maize profilin isoform, ZmPRO4, focusing on its expression, actin binding, poly-L-proline interaction, and cellular effects.
  • To compare the functional properties of ZmPRO4 with previously identified maize pollen profilin isoforms.
  • To investigate the role of poly-L-proline binding in profilin-mediated regulation of the actin cytoskeleton.

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Main Methods:

  • Quantitative analysis of ZmPRO4 expression across various maize tissues.
  • Measurement of ZmPRO4 affinity for monomeric actin and poly-L-proline using biochemical assays.
  • Microinjection of ZmPRO4 and a gain-of-function mutant (ZmPRO1-Y6F) into living plant cells.
  • Observation and quantification of effects on actin-dependent nuclear positioning and cytoarchitecture.

Main Results:

  • ZmPRO4 is primarily expressed in maize endosperm but present in other tissues, including pollen.
  • ZmPRO4 exhibits similar affinity for monomeric actin but a nearly twofold higher affinity for poly-L-proline compared to pollen profilins.
  • Microinjection of ZmPRO4 caused rapid alterations in actin-dependent nuclear positioning, exceeding the effect of ZmPRO1.
  • A ZmPRO1 mutant (ZmPRO1-Y6F) with enhanced poly-L-proline binding mimicked ZmPRO4's disruptive effects on cytoarchitecture.

Conclusions:

  • Different profilin isoforms expressed within the same plant cell can exert distinct regulatory effects on the actin cytoskeleton.
  • The enhanced poly-L-proline binding capability of ZmPRO4 is linked to its potent effects on actin dynamics and cellular organization.
  • Profilin's interaction with poly-L-proline represents a significant mechanism for controlling actin cytoskeletal dynamics in plant cells.