期刊
PLANT MOLECULAR BIOLOGY REPORTER
卷 29, 期 4, 页码 1006-1012出版社
SPRINGER
DOI: 10.1007/s11105-011-0296-3
关键词
Histidine triad nucleotide binding protein; Immune response; Maize; Molecular cloning; RT-PCR expression analysis
资金
- National Basic Research Program of China [2009CB118400]
- Science and Technology Development Programs of Henan Province [102102110171]
- China Postdoctoral Science Foundation [20100470993]
Histidine triad nucleotide binding protein (HINT1) belongs to a histidine triad (HIT) superfamily, which contains a highly conserved His-X-His-X-His-XX motif (X is a hydrophobic amino acid) and plays an important role in many biological processes. In this study, we have isolated the full-length cDNA of an HINT1 homologue from maize (Zea mays L.), designated as Zm-HINT1. The full-length cDNA of Zm-HINT1 consists of 729 bp with an ORF encoding a 138-amino acid protein. The deduced amino acid sequence of Zm-HINT1 shows high sequence homology to the mammalian HINT1 and contains conserved domains including the HIT motif, helical regions and beta-strands, which are the characteristics of HINT1 proteins. The phylogenetic analysis has revealed that Zm-HINT1 is branched along with Caenorhabditis elegans HINT1. RT-PCR analysis has revealed that Zm-HINT1 is ubiquitously expressed in maize tissues but not in the pericarp, thus suggesting that Zm-HINT1 may not be related to the production of fibrin. Furthermore, expression levels of Zm-HINT1 have increased rapidly following treatment with salicylic acid. Taken together, these results indicate that Zm-HINT1 is a mammalian HINT1 homologue and may be involved in the immune response of maize.
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