Journal of Experimental Botany, Vol. 54, No. 380, pp. 55-63,
January 1, 2003
© 2003 Oxford University Press
Characterization and localization of the transmitting tissue-specific PELPIII proteins of Nicotiana tabacum
Received 15 March 2002; Accepted 31 May 2002
Department of Experimental Botany, Laboratory of Plant Cell Biology, Graduate School of Experimental Plant Science, University of Nijmegen, Toernooiveld 1, 6525 ED, Nijmegen, The Netherlands
1 To whom correspondence should be addressed. Fax: +31 24 3652490. E-mail: Mariani@sci.kun.nl
2 Present address: Department of Biochemistry and Molecular Biology. J.W. Lederle Graduate Research Center, Box 34505, University of Massachusetts, Amherst, MA 01003-4505, USA.
The class III pistil-specific PELP proteins (PELPIII) of Nicotiana tabacum includes at least two members of highly soluble glycoproteins containing glucan modules that are characteristic for arabinogalactan proteins (AGPs). PELPIII accumulates in the style transmitting tissue (TT) during pistil development and, at flower anthesis, is present in the intercellular matrix (IM) of non-pollinated pistils. After pollination, PELPIII appears to be directly and completely translocated from the IM into the pollen tube callose walls, no significant accumulation was observed in the primary wall in the tip. In the spent parts of the pollen tubes these proteins become detectable against the remnants of the tube cell membrane and in the callose plugs. Different protein extraction procedures of PELPIII from pollinated tobacco pistils showed that these proteins remain in the highly soluble protein fraction and are not modified by the growing pollen tubes. These data concur with a role in IM development and pollen tube growth. In addition, the data show that the PELPIII are able to reach the cell membrane, facilitated by an already present or induced high porosity of the tube wall and an additional, yet unknown, mechanism. The differences in behaviour between the three related classes of style IM glycoproteins of Nicotiana, namely, PELPII, TTS and the120 kDa glycoprotein, are proposed to connect more to their differences in glycosylation than to major differences in amino acid sequence.
Key words: Callose, Nicotiana tabacum, PELPIII, pistil, pollen tube, transmitting tissue.
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