A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property
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 d...
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| Format: | Article |
| Language: | English English |
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Science Publications
2021
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| Online Access: | https://eprints.ums.edu.my/id/eprint/32951/1/A%20Meat-Derived%20Lactic%20Acid%20Bacteria%2C%20Lactobacillus%20plantarum%20IIA%2C%20Expresses%20a%20Functional%20Parvulin-Like%20Protein%20with%20Unique%20Structural%20Property.pdf https://eprints.ums.edu.my/id/eprint/32951/2/A%20Meat-Derived%20Lactic%20Acid%20Bacteria%2C%20Lactobacillus%20plantarum%20IIA%2C%20Expresses%20a%20Functional%20Parvulin-Like%20Protein%20with%20Unique%20Structural%20Property1.pdf |
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| author | Cahyo Budiman Irma Isnafia Arief Fernandes Opook Muhammad Yusuf |
| author_facet | Cahyo Budiman Irma Isnafia Arief Fernandes Opook Muhammad Yusuf |
| author_sort | Cahyo Budiman |
| collection | UMS |
| description | 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. |
| first_indexed | 2024-03-06T03:17:02Z |
| format | Article |
| id | ums.eprints-32951 |
| institution | Universiti Malaysia Sabah |
| language | English English |
| last_indexed | 2024-03-06T03:17:02Z |
| publishDate | 2021 |
| publisher | Science Publications |
| record_format | dspace |
| spelling | ums.eprints-329512022-06-23T05:58:59Z https://eprints.ums.edu.my/id/eprint/32951/ A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property Cahyo Budiman Irma Isnafia Arief Fernandes Opook Muhammad Yusuf QP501-801 Animal biochemistry 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. Science Publications 2021 Article PeerReviewed text en https://eprints.ums.edu.my/id/eprint/32951/1/A%20Meat-Derived%20Lactic%20Acid%20Bacteria%2C%20Lactobacillus%20plantarum%20IIA%2C%20Expresses%20a%20Functional%20Parvulin-Like%20Protein%20with%20Unique%20Structural%20Property.pdf text en https://eprints.ums.edu.my/id/eprint/32951/2/A%20Meat-Derived%20Lactic%20Acid%20Bacteria%2C%20Lactobacillus%20plantarum%20IIA%2C%20Expresses%20a%20Functional%20Parvulin-Like%20Protein%20with%20Unique%20Structural%20Property1.pdf Cahyo Budiman and Irma Isnafia Arief and Fernandes Opook and Muhammad Yusuf (2021) A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property. OnLine Journal of Biological Sciences, 21. pp. 120-135. ISSN 1608-4217 https://thescipub.com/abstract/ojbsci.2021.120.135 https://doi.org/10.3844/ojbsci.2021.120.135 https://doi.org/10.3844/ojbsci.2021.120.135 |
| spellingShingle | QP501-801 Animal biochemistry Cahyo Budiman Irma Isnafia Arief Fernandes Opook Muhammad Yusuf A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property |
| title | A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property |
| title_full | A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property |
| title_fullStr | A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property |
| title_full_unstemmed | A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property |
| title_short | A Meat-Derived Lactic Acid Bacteria, Lactobacillus plantarum IIA, Expresses a Functional Parvulin-Like Protein with Unique Structural Property |
| title_sort | meat derived lactic acid bacteria lactobacillus plantarum iia expresses a functional parvulin like protein with unique structural property |
| topic | QP501-801 Animal biochemistry |
| url | https://eprints.ums.edu.my/id/eprint/32951/1/A%20Meat-Derived%20Lactic%20Acid%20Bacteria%2C%20Lactobacillus%20plantarum%20IIA%2C%20Expresses%20a%20Functional%20Parvulin-Like%20Protein%20with%20Unique%20Structural%20Property.pdf https://eprints.ums.edu.my/id/eprint/32951/2/A%20Meat-Derived%20Lactic%20Acid%20Bacteria%2C%20Lactobacillus%20plantarum%20IIA%2C%20Expresses%20a%20Functional%20Parvulin-Like%20Protein%20with%20Unique%20Structural%20Property1.pdf |
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