Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings
A full-length cDNA clone encoding cyclophilin gene of 848 bp, including a 519 bp open reading frame, has been isolated from the cDNA library constructed from etiolated seedlings of Vigna mungo (GenBank FN668732). The cDNA sequence showed 97% identity with Vigna radiata cyclophilin mRNA. The sequence was GC rich and lacked introns. The open reading frame encoded 172 amino acid polypeptide with molecular weight 18.3 kDa and theoretical pI 8.61. BlastP analysis indicated that its putative amino acid sequence shared 100% identity with several plant cyclophilins particularly legumes. The conserved seven amino acid residues region in V. mungo cyclophilin was RSGKPLH (present in legumes) instead of KSGKPLH, indicating its similarity to the cyclophilins of other legumes. This novel V. mungo cyclophilin gene will broaden the pool of plant cyclophilin genes for further studies.
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Brazilian Journal of Plant Physiology
2012
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oai:scielo:S1677-042020120001000092012-10-04Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlingsKuhar,KalikaGupta,Varun KumarKansal,RekhaGupta,Vijay Kumar gene library open reading frame A full-length cDNA clone encoding cyclophilin gene of 848 bp, including a 519 bp open reading frame, has been isolated from the cDNA library constructed from etiolated seedlings of Vigna mungo (GenBank FN668732). The cDNA sequence showed 97% identity with Vigna radiata cyclophilin mRNA. The sequence was GC rich and lacked introns. The open reading frame encoded 172 amino acid polypeptide with molecular weight 18.3 kDa and theoretical pI 8.61. BlastP analysis indicated that its putative amino acid sequence shared 100% identity with several plant cyclophilins particularly legumes. The conserved seven amino acid residues region in V. mungo cyclophilin was RSGKPLH (present in legumes) instead of KSGKPLH, indicating its similarity to the cyclophilins of other legumes. This novel V. mungo cyclophilin gene will broaden the pool of plant cyclophilin genes for further studies.info:eu-repo/semantics/openAccessBrazilian Journal of Plant PhysiologyBrazilian Journal of Plant Physiology v.24 n.1 20122012-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202012000100009en10.1590/S1677-04202012000100009 |
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Kuhar,Kalika Gupta,Varun Kumar Kansal,Rekha Gupta,Vijay Kumar |
| spellingShingle |
Kuhar,Kalika Gupta,Varun Kumar Kansal,Rekha Gupta,Vijay Kumar Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings |
| author_facet |
Kuhar,Kalika Gupta,Varun Kumar Kansal,Rekha Gupta,Vijay Kumar |
| author_sort |
Kuhar,Kalika |
| title |
Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings |
| title_short |
Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings |
| title_full |
Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings |
| title_fullStr |
Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings |
| title_full_unstemmed |
Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings |
| title_sort |
isolation and in silico characterization of cdna encoding cyclophilin from etiolated vigna mungo seedlings |
| description |
A full-length cDNA clone encoding cyclophilin gene of 848 bp, including a 519 bp open reading frame, has been isolated from the cDNA library constructed from etiolated seedlings of Vigna mungo (GenBank FN668732). The cDNA sequence showed 97% identity with Vigna radiata cyclophilin mRNA. The sequence was GC rich and lacked introns. The open reading frame encoded 172 amino acid polypeptide with molecular weight 18.3 kDa and theoretical pI 8.61. BlastP analysis indicated that its putative amino acid sequence shared 100% identity with several plant cyclophilins particularly legumes. The conserved seven amino acid residues region in V. mungo cyclophilin was RSGKPLH (present in legumes) instead of KSGKPLH, indicating its similarity to the cyclophilins of other legumes. This novel V. mungo cyclophilin gene will broaden the pool of plant cyclophilin genes for further studies. |
| publisher |
Brazilian Journal of Plant Physiology |
| publishDate |
2012 |
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http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202012000100009 |
| work_keys_str_mv |
AT kuharkalika isolationandinsilicocharacterizationofcdnaencodingcyclophilinfrometiolatedvignamungoseedlings AT guptavarunkumar isolationandinsilicocharacterizationofcdnaencodingcyclophilinfrometiolatedvignamungoseedlings AT kansalrekha isolationandinsilicocharacterizationofcdnaencodingcyclophilinfrometiolatedvignamungoseedlings AT guptavijaykumar isolationandinsilicocharacterizationofcdnaencodingcyclophilinfrometiolatedvignamungoseedlings |
| _version_ |
1756427693426999296 |