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<mods ID="bpl-201802-0007">
	<titleInfo><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></titleInfo>
	<name type="personal">
		<namePart type="family">Rojas</namePart>
		<namePart type="given">H. J.</namePart>
		<role><roleTerm type="text">author</roleTerm></role>
	</name>
	<name type="personal">
		<namePart type="family">Caspani</namePart>
		<namePart type="given">C.</namePart>
		<role><roleTerm type="text">author</roleTerm></role>
	</name>
	<name type="personal">
		<namePart type="family">Escobar</namePart>
		<namePart type="given">E. G.</namePart>
		<role><roleTerm type="text">author</roleTerm></role>
	</name>
	<name type="personal">
		<namePart type="family">Quiroga</namePart>
		<namePart type="given">R.</namePart>
		<role><roleTerm type="text">author</roleTerm></role>
	</name>
	<name type="personal">
		<namePart type="family">Goldraij</namePart>
		<namePart type="given">A.</namePart>
		<role><roleTerm type="text">author</roleTerm></role>
	</name>
	<typeOfResource>text</typeOfResource>
	<genre>journal article</genre>
	<originInfo><dateIssued>2018</dateIssued></originInfo>
	<language></language>
	<abstract lang="English">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>
	<subject><topic>ribonuclease; self-incompatibility; S-locus; stress responses</topic></subject>
	<identifier type="doi">10.1007/s10535-018-0783-6</identifier>
	<identifier type="uri">https://bp.ueb.cas.cz/artkey/bpl-201802-0007.php</identifier>
	<location><url>https://bp.ueb.cas.cz/artkey/bpl-201802-0007.php</url></location>
	<relatedItem type="host">
		<titleInfo><title>Biologia plantarum</title></titleInfo>
		<originInfo><issuance>continuing</issuance></originInfo>
		<part>
			<detail type="volume"><number>62</number></detail>
			<detail type="issue"><number>2</number></detail>
			<extent unit="pages">
				<start>261</start>
				<end>268</end>
			</extent>
			<date>2018</date>
		</part>
		<identifier type="issn"></identifier>
		<genre authority="marc">periodical</genre>
		<genre>academic journal</genre>
	</relatedItem>
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