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J Plant Physiol. 2013 Oct 15;170(15):1384-8. doi: 10.1016/j.jplph.2013.05.001. Epub 2013 Jun 7.

Characterization of PhPRP1, a histidine domain arabinogalactan protein from Petunia hybrida pistils.

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Biology Department, Western Washington University, Bellingham, WA, USA.


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).


Arabinogalactan protein; ECM; HD-AGP; Petunia; Pollen; Solanaceae; TTS protein; extracellular matrix; histidine domain-arabinogalactan protein; transmitting tissue-specific protein

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