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<ArticleSet>
<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>7</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2018</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Cloning and molecular characterization of TaERF6, a gene encoding a bread wheat ethylene response factor</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>153</FirstPage>
			<LastPage>163</LastPage>
			<ELocationID EIdType="pii">5035</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2018.30339.1336</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Shahrzad</FirstName>
					<LastName>Haghir</LastName>
<Affiliation>Department of Crop Production and Plant Breeding, School of Agriculture, Shiraz University, Shiraz, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Abbas</FirstName>
					<LastName>Alemzadeh</LastName>
<Affiliation>Department of Crop Production and Plant Breeding, School of Agriculture, Shiraz University, Shiraz, Iran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2018</Year>
					<Month>07</Month>
					<Day>31</Day>
				</PubDate>
			</History>
		<Abstract>Ethylene response factor proteins are important for regulating gene expression under different stresses. Different isoforms for ERF have previously isolated from bread wheat (&lt;em&gt;Triticum aestivum&lt;/em&gt; L.) and related genera and called from &lt;em&gt;TaERF1&lt;/em&gt; to &lt;em&gt;TaERF5&lt;/em&gt;. We isolated, cloned and molecular characterized a novel one based on &lt;em&gt;TdERF1&lt;/em&gt;, an isoform in durum wheat (&lt;em&gt;Triticum turgidum&lt;/em&gt; L.) and called &lt;em&gt;TaERF6&lt;/em&gt;. Its cDNA was synthesized, sequenced and compared with genomic sequence to figure out intron and exon regions and determine coding sequence region. The length of &lt;em&gt;TdERF1&lt;/em&gt; gene was 1939 bp and cDNA was 1065 bp including two exons, the first one 259 bp and the second one 806 bp separated by a 874 bp intron with a 111 bp 5&#039;-UTR (untranslated region) and 401 bp 3&#039;-UTR. &lt;em&gt;TaERF6&lt;/em&gt; encodes a 353 amino acids protein with nearly 99% identity to TdERF1. Hydrophobic cluster analysis revealed an N-terminal hydrophobic domain contains a highly conserved motif with the consensus sequence of M [C/L/Y] [G/R] [G/R/P] [A/G/V/L/R] [I/L/R/S/P/Q] [L/I/R/H] and hydrophobic clusters in AP2/ERF domain of which tends to form b-sheet. Three monopartite nuclear localization signals also identified in TaERF6 that play important role in getting back into the nucleus. The results showed several putative phosphorylation sites in TaERF6 that a motif from residues 246 to 266, the CMVII-4 motif, was predicted to phosphorylate by different kinase proteins and play important roles in TaERF6 function. Phylogenetic analysis showed 7 clusters (I to VII) and 10 subclusters according to their relatedness in Poaceae family.</Abstract>
		<ObjectList>
			<Object Type="keyword">
			<Param Name="value">Hydrophobic cluster analysis</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Phosphorylation sites</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Phylogenetic</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Poaceae</Param>
			</Object>
		</ObjectList>
<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_5035_b5340537cf2da8653e029b5a090dbeaa.pdf</ArchiveCopySource>
</Article>
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