Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions
Glutathione S-Transferases (GSTs) comprise a diverse group of protein superfamily involved in cellular detoxification of various harmful xenobiotics and endobiotics. Cyanobacteria, being the primordial photosynthetic prokaryotes, served as an origin for the evolution of GSTs with diversity in their...
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MDPI AG
2020-05-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/8/5/712 |
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| author | Mohandass ShylajaNaciyar Lakshmanan Karthick Peter Arul Prakasam Garlapati Deviram Lakshmanan Uma Dharmar Prabaharan Sushanta Kumar Saha |
| author_facet | Mohandass ShylajaNaciyar Lakshmanan Karthick Peter Arul Prakasam Garlapati Deviram Lakshmanan Uma Dharmar Prabaharan Sushanta Kumar Saha |
| author_sort | Mohandass ShylajaNaciyar |
| collection | DOAJ |
| description | Glutathione S-Transferases (GSTs) comprise a diverse group of protein superfamily involved in cellular detoxification of various harmful xenobiotics and endobiotics. Cyanobacteria, being the primordial photosynthetic prokaryotes, served as an origin for the evolution of GSTs with diversity in their structures, substrate recognition, and catalytic functions. This study analysed the diversity of GSTs in cyanobacteria for the first time. Based on the sequence alignment and phylogenetic tree analysis, 12 GST classes were identified, which are distributed variedly within cyanobacterial orders such as four in <i>Pleurocapsales</i>, eight in <i>Chroococcales</i>, seven in <i>Oscillatoriales</i>, five in <i>Stigonematales</i>, and nine in <i>Nostocales</i>. Detailed evolutionary analysis of cyanobacterial GSTs suggested that the order <i>Pleurocapsales</i> served as the ancestry for GST evolution. The analysis also identified a conserved motif S[GLNTARS][ADE]I[LAI] with signature residues, cysteine, serine, and tyrosine at the N-terminal end that serves as the initiating residue for detoxification. Alternatively, the grouping of cyanobacterial GSTs and their unique signature residues were located, which serve as a possible discriminating factor. The study also described the mode of glutathione binding between the identified cyanobacterial GST groups highlighting the differences among the GST classes. New GST sequence data may improve further our understanding on GST evolution and other possible divergences in cyanobacteria. |
| first_indexed | 2024-03-10T19:55:00Z |
| format | Article |
| id | doaj.art-f2d19a702dfa42e7ac577a0946f0333e |
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| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T19:55:00Z |
| publishDate | 2020-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-f2d19a702dfa42e7ac577a0946f0333e2023-11-20T00:04:58ZengMDPI AGMicroorganisms2076-26072020-05-018571210.3390/microorganisms8050712Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic FunctionsMohandass ShylajaNaciyar0Lakshmanan Karthick1Peter Arul Prakasam2Garlapati Deviram3Lakshmanan Uma4Dharmar Prabaharan5Sushanta Kumar Saha6Department of Marine Biotechnology, School of Marine Sciences, National Facility for Marine Cyanobacteria (Sponsored by DBT, Govt. of India), Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, IndiaDepartment of Marine Biotechnology, School of Marine Sciences, National Facility for Marine Cyanobacteria (Sponsored by DBT, Govt. of India), Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, IndiaDepartment of Marine Biotechnology, School of Marine Sciences, National Facility for Marine Cyanobacteria (Sponsored by DBT, Govt. of India), Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, IndiaDepartment of Marine Biotechnology, School of Marine Sciences, National Facility for Marine Cyanobacteria (Sponsored by DBT, Govt. of India), Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, IndiaDepartment of Marine Biotechnology, School of Marine Sciences, National Facility for Marine Cyanobacteria (Sponsored by DBT, Govt. of India), Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, IndiaDepartment of Marine Biotechnology, School of Marine Sciences, National Facility for Marine Cyanobacteria (Sponsored by DBT, Govt. of India), Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, IndiaShannon Applied Biotechnology Centre, Limerick Institute of Technology, Moylish Park, Limerick V94 E8YF, Ireland (ROI)Glutathione S-Transferases (GSTs) comprise a diverse group of protein superfamily involved in cellular detoxification of various harmful xenobiotics and endobiotics. Cyanobacteria, being the primordial photosynthetic prokaryotes, served as an origin for the evolution of GSTs with diversity in their structures, substrate recognition, and catalytic functions. This study analysed the diversity of GSTs in cyanobacteria for the first time. Based on the sequence alignment and phylogenetic tree analysis, 12 GST classes were identified, which are distributed variedly within cyanobacterial orders such as four in <i>Pleurocapsales</i>, eight in <i>Chroococcales</i>, seven in <i>Oscillatoriales</i>, five in <i>Stigonematales</i>, and nine in <i>Nostocales</i>. Detailed evolutionary analysis of cyanobacterial GSTs suggested that the order <i>Pleurocapsales</i> served as the ancestry for GST evolution. The analysis also identified a conserved motif S[GLNTARS][ADE]I[LAI] with signature residues, cysteine, serine, and tyrosine at the N-terminal end that serves as the initiating residue for detoxification. Alternatively, the grouping of cyanobacterial GSTs and their unique signature residues were located, which serve as a possible discriminating factor. The study also described the mode of glutathione binding between the identified cyanobacterial GST groups highlighting the differences among the GST classes. New GST sequence data may improve further our understanding on GST evolution and other possible divergences in cyanobacteria.https://www.mdpi.com/2076-2607/8/5/712cyanobacteriaglutathione S-Transferases (GSTs)detoxification |
| spellingShingle | Mohandass ShylajaNaciyar Lakshmanan Karthick Peter Arul Prakasam Garlapati Deviram Lakshmanan Uma Dharmar Prabaharan Sushanta Kumar Saha Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions Microorganisms cyanobacteria glutathione S-Transferases (GSTs) detoxification |
| title | Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions |
| title_full | Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions |
| title_fullStr | Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions |
| title_full_unstemmed | Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions |
| title_short | Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions |
| title_sort | diversity of glutathione s transferases gsts in cyanobacteria with reference to their structures substrate recognition and catalytic functions |
| topic | cyanobacteria glutathione S-Transferases (GSTs) detoxification |
| url | https://www.mdpi.com/2076-2607/8/5/712 |
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