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Characterization and localization of the transmitting tissue‐specific PELPIII proteins of Nicotiana tabacum

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 deve...

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Bibliographic Details
Published in:Journal of experimental botany 2003-01, Vol.54 (380), p.55-63
Main Authors: de Graaf, B. H. J., Knuiman, B. A., Derksen, J., Mariani, C.
Format: Article
Language:English
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Summary: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.
ISSN:0022-0957
1460-2431
DOI:10.1093/jxb/erg002