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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 392, Issue 3

Issues

Identification of lily pollen 14-3-3 isoforms and their subcellular and time-dependent expression profile

Heidi Pertl
  • Molecular Plant Biophysics and Biochemistry, Department of Molecular Biology, University of Salzburg, Billrothstr. 11, A-5020 Salzburg, Austria
  • Other articles by this author:
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/ Simon Rittmann
  • Molecular Plant Biophysics and Biochemistry, Department of Molecular Biology, University of Salzburg, Billrothstr. 11, A-5020 Salzburg, Austria
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Waltraud X. Schulze / Gerhard Obermeyer
  • Molecular Plant Biophysics and Biochemistry, Department of Molecular Biology, University of Salzburg, Billrothstr. 11, A-5020 Salzburg, Austria
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Published Online: 2011-06-18 | DOI: https://doi.org/10.1515/bc.2011.026

Abstract

14-3-3 proteins are major regulators in plant development and physiology including primary metabolism and signal transduction pathways, typically via a phosphorylation-dependent interaction with a target protein. Four full-length 14-3-3 isoforms were identified in pollen grains of Lilium longiflorum by screening of a cDNA library and RACE (rapid amplification of cDNA ends)-PCR. Mass spectrometry analysis of partially purified 14-3-3s confirmed the presence of the four isoforms but also indicated the presence of additional, less abundant 14-3-3 isoforms in lily pollen. Separation of partially purified 14-3-3 proteins by two-dimensional gel electrophoresis resulted in nine spots that mainly contained the four major 14-3-3 isoforms. In a first step to examine putative physiological roles of specific 14-3-3 isoforms, their subcellular expression profile during pollen germination and tube growth was monitored using a characterized set of antibodies against 14-3-3 proteins with distinct crossreactivity. The abundance profile of 14-3-3 proteins associated with the cytosol, endomembranes (tonoplast, endoplasmic reticulum, Golgi, mitochondria) and plasma membrane showed high spatial-temporal dynamics. This indicates different targets of 14-3-3 proteins at different organelles and time points during pollen germination and growth.

Keywords: 14-3-3 protein; Lilium longiflorum; mass spectrometry; protein-protein interaction; spatial-temporal dynamics; tip growth

About the article

Corresponding author


Received: 2010-09-09

Accepted: 2010-10-25

Published Online: 2011-06-18

Published in Print: 2011-03-01


Citation Information: Biological Chemistry, Volume 392, Issue 3, Pages 249–262, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2011.026.

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