| Literature DB >> 28058638 |
Eirini-Evangelia Thomloudi1, Aggeliki Skagia1, Anastasia Venieraki1, Panagiotis Katinakis1, Maria Dimou2.
Abstract
The nitrogen fixing Sinorhizobium meliloti possesses two genes, ppiA and ppiB, encoding two cyclophilin isoforms which belong to the superfamily of peptidyl prolyl cis/trans isomerases (PPIase, EC: 5.2.1.8). Here, we functionally characterize the two proteins and we demonstrate that both recombinant cyclophilins are able to isomerise the Suc-AAPF-pNA synthetic peptide but neither of them displays chaperone function in the citrate synthase thermal aggregation assay. Furthermore, we observe that the expression of both enzymes increases the viability of E. coli BL21 in the presence of abiotic stress conditions such as increased heat and salt concentration. Our results support and strengthen previous high-throughput studies implicating S. meliloti cyclophilins in various stress conditions.Entities:
Keywords: Abiotic stress; Cyclophilin; Peptidyl-prolyl cis/trans isomerase; Sinorhizobium meliloti
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Year: 2017 PMID: 28058638 DOI: 10.1007/s11274-016-2201-6
Source DB: PubMed Journal: World J Microbiol Biotechnol ISSN: 0959-3993 Impact factor: 3.312