Isolation and in silico characterization of cDNA encoding cyclophilin from etiolated Vigna mungo seedlings

AUTOR(ES)

Kuhar, Kalika, Gupta, Varun Kumar, Kansal, Rekha, Gupta, Vijay Kumar

FONTE

Braz. J. Plant Physiol.

DATA DE PUBLICAÇÃO

2012

RESUMO

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.

Documentos Relacionados

• cDNA for catalase from etiolated mung bean (Vigna radiata) hypocotyls.
• Nucleotide sequence of cDNA for alpha-amylase from cotyledons of germinating Vigna mungo seeds.
• Isolation and characterization of the cDNA encoding human DNA methyltransferase.
• Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds.
• Isolation and characterization of a cDNA clone encoding a lectin gene from Agaricus bisporus.