A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property
- 1 Department of Animal Production and Technology, Faculty of Animal Science, IPB University, Jl Kampus IPB Darmaga, Bogor, 16680, Indonesia
- 2 Biotechnology Research Institute, Universiti Malaysia Sabah, Jl UMS 88400, Kota Kinabalu, Malaysia
Abstract
The genome sequence of a Lactic Acid Bacterium (LAB) Lactobacillus plantarum IIA contains a single gene encoding a parvulin-like protein (Par-LpIIA). This protein belongs to Peptidyl Prolyl cis-trans Isomerase (PPIase) family proteins that catalyze a slow cis-trans isomerization of cis prolyl bond during protein folding. This study aims to provide molecular and biochemical evidences of the existence of Par-LpIIA in L. plantarum IIA and have an insight into its structural properties. The result showed that the gene encoding Par-LpIIA was successfully amplified using specific primers yielding a ~900 bp amplicon indicating that the gene indeed exists in its genomic DNA. BLAST analysis confirmed that the protein is a rotamase of parvulin-like protein. Further biochemical analysis demonstrated that cell lysate of L. plantarum IIA-1A5 exhibited remarkable PPIase activity towards peptide substrate and ability to accelerate the refolding of RNase T1, with the catalytic efficiency (kcat/KM) of 1.9 and 0.02 µM-1 s-1, respectively. A specific inhibitor clearly inhibited the PPIase activity for parvulin-like protein with IC50 of 230 nM confirming that the protein encoded by Par-LpIIA gene is a parvulin-like protein and expressed in an active form. Further, the three-dimensional model of Par-LpIIA showed that this protein consists of two domains of a homolog WW domain and PPIase domain with a unique active site configuration compared to human Pin1. Altogether, we then proposed the possible roles of this protein for L. plantarum IIA.
DOI: https://doi.org/10.3844/ojbsci.2021.120.135
Copyright: © 2021 Cahyo Budiman, Irma Isnafia Arief, Fernandes Opook and Muhammad Yusuf. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Keywords
- Peptidyl Prolyl cis-trans Isomerase
- Lactobacillus plantarum
- Parvulin
- Active Site
- Structural Homology Modelling