<?xml version="1.0" encoding="UTF-8"?>
<xml>
<records>
<record>
	<source-app name="Actavia">Actavia</source-app>
	<ref-type name="Journal Article">0</ref-type>
	<contributors>
		<authors>
			<author>Rojas, H. J.</author>
			<author>Caspani, C.</author>
			<author>Escobar, E. G.</author>
			<author>Quiroga, R.</author>
			<author>Goldraij, A.</author>
		</authors>
		<secondary-authors></secondary-authors>
	</contributors>
	<titles><title>NaPi/S&lt;sub&gt;X&lt;/sub&gt;-RNase segregates as a functional S-RNase and is induced under phosphate deficiency in Nicotiana alata</title></titles>
	<dates>
		<year>2018</year>
		<pub-dates><date>2018-6-1</date></pub-dates>
	</dates>
	<pages>261-268</pages>
	<abstract>In plants, class III T2 RNases involves two groups of structurally similar proteins, but with different biological functions: S-RNases and non-S-RNases. S-RNases have been involved in self-incompatibility whereas non-S-RNases have been implicated in stress responses. Here we report a novel class III RNase termed NaPi/S&lt;sub&gt;x&lt;/sub&gt;-RNase, which works both in self-incompatibility and in response to phosphate deficiency. The NaPi/S&lt;sub&gt;x&lt;/sub&gt;-RNase gene was identified in roots of Nicotiana alata grown in the absence of inorganic phosphate. Phylogenetic analysis showed that NaPi/S&lt;sub&gt;x&lt;/sub&gt;-RNase was included within the class III RNase T2 group. The NaPi/S&lt;sub&gt;x&lt;/sub&gt;-RNase was expressed in styles and its temporal expression increased in parallel to stylar development, with a slight decrease after anthesis. Progeny analysis showed that NaPi/S&lt;sub&gt;x&lt;/sub&gt;-RNase and S&lt;sub&gt;107&lt;/sub&gt;-RNase, a functional allele of the self-incompatibility system, segregated in a 1:1 ratio. The progeny segregation of a semicompatible cross, in which NaPi/S&lt;sub&gt;x&lt;/sub&gt;-RNase was shared by the two parents, exhibited a pattern consistent with a functional S-RNase allele. Considering genetic segregation, primary structure, and physiological role, the NaPi/S&lt;sub&gt;x&lt;/sub&gt;-RNase may be either an S-RNase with diversified functions or a non-S-RNase linked to the S-locus. To our knowledge, this is the first evidence for a specific function of the S-locus other than the self-incompatibility reaction. These results support the hypothesis that the self-incompatibility and stress responses may have evolved from a common origin.</abstract>
	<number>2</number>
	<volume>62</volume>
</record>
</records>
</xml>
