Characterization of PhPRP1, a histidine domain arabinogalactan protein from Petunia hybrida pistils
Copyright © 2013 Elsevier GmbH. All rights reserved.
| Publié dans: | Journal of plant physiology. - 1979. - 170(2013), 15 vom: 15. Okt., Seite 1384-8 |
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| Auteur principal: | |
| Autres auteurs: | , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2013
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| Accès à la collection: | Journal of plant physiology |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Arabinogalactan protein ECM HD-AGP Petunia Pollen Solanaceae TTS protein extracellular matrix plus... |
| Résumé: | Copyright © 2013 Elsevier GmbH. All rights reserved. An arabinogalactan protein, PhPRP1, was purified from Petunia hybrida pistils and shown to be orthologous to TTS-1 and TTS-2 from Nicotiana tabacum and NaTTS from Nicotiana alata. Sequence comparisons among these proteins, and CaPRP1 from Capsicum annuum, reveal a conserved histidine-rich domain and two hypervariable domains. Immunoblots show that TTS-1 and PhPRP1 are also expressed in vegetative tissues of tobacco and petunia respectively. In contrast to the molecular mass heterogeneity displayed by the pistil proteins, the different isoforms found in seedlings, roots, and leaves each has a discrete size (37, 80, 160, and 200 kDa) on SDS-PAGE gels. On the basis of their chemistry, distinctive domain architecture, and the unique pattern of expression, we have named this group of proteins HD-AGPs (histidine domain-arabinogalactan proteins) |
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| Description: | Date Completed 13.03.2014 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1618-1328 |
| DOI: | 10.1016/j.jplph.2013.05.001 |