Abstract
Gyrases are a class of Topoisomerase II that facilitate ATP dependent negative supercoiling of DNA during transcription and replication. They aid in strand breakage during chromosome condensation and take part in separation of intertwined DNA during mitosis. The present study reports gyrase-A (PsGryA) CDS clone from Pisum sativum (L.) comprising of 2817 bp that encodes for a peptide of 939 amino acids. The estimated molecular weight of PsGryA is approximately 104 kDa with pI as 6.99. The protein sequence showed maximum similarity with GyrA of Medicago truncatula. The PsGyrA polypeptide has approximately 42% overall sequence identity with Escherichia coli gyrase-A. The three-dimensional structure of PsGyrA generated based on the X-ray structure of E. coli gyrase-A revealed a putative active site region with amino acid (AA) sequence AAMRYTE located between 208th and 214th AA with a tyrosine residue at position 212. In silico and In vivo immunolocalization studies establishes the dual targeting of PsGyrA to both chloroplast and mitochondria.
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