The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte

<p>Abstract</p> <p>Background</p> <p>The tomato kinase Pto confers resistance to bacterial speck disease caused by <it>Pseudomonas syringae </it>pv. <it>tomato </it>in a gene for gene manner. Upon recognition of specific avirulence factors the Pt...

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Main Authors: Wienand Udo, Kluth Jantjeline, Pinto Sheena, Herrmann Markus M, Lorbiecke René
Format: Article
Language:English
Published: BMC 2006-10-01
Series:BMC Plant Biology
Online Access:http://www.biomedcentral.com/1471-2229/6/22
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author Wienand Udo
Kluth Jantjeline
Pinto Sheena
Herrmann Markus M
Lorbiecke René
author_facet Wienand Udo
Kluth Jantjeline
Pinto Sheena
Herrmann Markus M
Lorbiecke René
author_sort Wienand Udo
collection DOAJ
description <p>Abstract</p> <p>Background</p> <p>The tomato kinase Pto confers resistance to bacterial speck disease caused by <it>Pseudomonas syringae </it>pv. <it>tomato </it>in a gene for gene manner. Upon recognition of specific avirulence factors the Pto kinase activates multiple signal transduction pathways culminating in induction of pathogen defense. The soluble cytoplasmic serine/threonine kinase Pti1 is one target of Pto phosphorylation and is involved in the hypersensitive response (HR) reaction. However, a clear role of Pti1 in plant pathogen resistance is uncertain. So far, no Pti1 homologues from monocotyledonous species have been studied.</p> <p>Results</p> <p>Here we report the identification and molecular analysis of four Pti1-like kinases from maize (ZmPti1a, -b, -c, -d). These kinase genes showed tissue-specific expression and their corresponding proteins were targeted to different cellular compartments. Sequence similarity, expression pattern and cellular localization of ZmPti1b suggested that this gene is a putative orthologue of Pti1 from tomato. In contrast, ZmPti1a was specifically expressed in pollen and sequestered to the plasma membrane, evidently owing to N-terminal modification by myristoylation and/or S-acylation. The ZmPti1a:GFP fusion protein was not evenly distributed at the pollen plasma membrane but accumulated as an annulus-like structure which co-localized with callose (1,3-β-glucan) deposition. In addition, co-localization of ZmPti1a and callose was observed during stages of pollen mitosis I and pollen tube germination. Maize plants in which ZmPti1a expression was silenced by RNA interference (RNAi) produced pollen with decreased competitive ability. Hence, our data provide evidence that ZmPti1a plays an important part in a signalling pathway that accelerates pollen performance and male fitness.</p> <p>Conclusion</p> <p>ZmPti1a from maize is involved in pollen-specific processes during the progamic phase of reproduction, probably in crucial signalling processes associated with regions of callose deposition. Pollen-sporophyte interactions and pathogen induced HR show certain similarities. For example, HR has been shown to be associated with cell wall reinforcement through callose deposition. Hence, it is hypothesized that Pti1 kinases from maize act as general components in evolutionary conserved signalling processes associated with callose, however during different developmental programs and in different tissue types.</p>
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spelling doaj.art-2924be821a924044906e2c7f3a7601402022-12-21T23:20:29ZengBMCBMC Plant Biology1471-22292006-10-01612210.1186/1471-2229-6-22The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyteWienand UdoKluth JantjelinePinto SheenaHerrmann Markus MLorbiecke René<p>Abstract</p> <p>Background</p> <p>The tomato kinase Pto confers resistance to bacterial speck disease caused by <it>Pseudomonas syringae </it>pv. <it>tomato </it>in a gene for gene manner. Upon recognition of specific avirulence factors the Pto kinase activates multiple signal transduction pathways culminating in induction of pathogen defense. The soluble cytoplasmic serine/threonine kinase Pti1 is one target of Pto phosphorylation and is involved in the hypersensitive response (HR) reaction. However, a clear role of Pti1 in plant pathogen resistance is uncertain. So far, no Pti1 homologues from monocotyledonous species have been studied.</p> <p>Results</p> <p>Here we report the identification and molecular analysis of four Pti1-like kinases from maize (ZmPti1a, -b, -c, -d). These kinase genes showed tissue-specific expression and their corresponding proteins were targeted to different cellular compartments. Sequence similarity, expression pattern and cellular localization of ZmPti1b suggested that this gene is a putative orthologue of Pti1 from tomato. In contrast, ZmPti1a was specifically expressed in pollen and sequestered to the plasma membrane, evidently owing to N-terminal modification by myristoylation and/or S-acylation. The ZmPti1a:GFP fusion protein was not evenly distributed at the pollen plasma membrane but accumulated as an annulus-like structure which co-localized with callose (1,3-β-glucan) deposition. In addition, co-localization of ZmPti1a and callose was observed during stages of pollen mitosis I and pollen tube germination. Maize plants in which ZmPti1a expression was silenced by RNA interference (RNAi) produced pollen with decreased competitive ability. Hence, our data provide evidence that ZmPti1a plays an important part in a signalling pathway that accelerates pollen performance and male fitness.</p> <p>Conclusion</p> <p>ZmPti1a from maize is involved in pollen-specific processes during the progamic phase of reproduction, probably in crucial signalling processes associated with regions of callose deposition. Pollen-sporophyte interactions and pathogen induced HR show certain similarities. For example, HR has been shown to be associated with cell wall reinforcement through callose deposition. Hence, it is hypothesized that Pti1 kinases from maize act as general components in evolutionary conserved signalling processes associated with callose, however during different developmental programs and in different tissue types.</p>http://www.biomedcentral.com/1471-2229/6/22
spellingShingle Wienand Udo
Kluth Jantjeline
Pinto Sheena
Herrmann Markus M
Lorbiecke René
The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
BMC Plant Biology
title The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
title_full The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
title_fullStr The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
title_full_unstemmed The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
title_short The PTI1-like kinase ZmPti1a from maize (<it>Zea mays </it>L.) co-localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
title_sort pti1 like kinase zmpti1a from maize it zea mays it l co localizes with callose at the plasma membrane of pollen and facilitates a competitive advantage to the male gametophyte
url http://www.biomedcentral.com/1471-2229/6/22
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