A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues
Rolling circle replication (RCR) is ubiquitously used by cellular and viral systems for genome and plasmid replication. While the molecular mechanism of RCR has been described, the structural mechanism is desperately lacking. Circular-rep encoded single stranded DNA (CRESS-DNA) viruses employ a vira...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-12-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/14/1/37 |
| _version_ | 1797489781041528832 |
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| author | Elvira Tarasova Reza Khayat |
| author_facet | Elvira Tarasova Reza Khayat |
| author_sort | Elvira Tarasova |
| collection | DOAJ |
| description | Rolling circle replication (RCR) is ubiquitously used by cellular and viral systems for genome and plasmid replication. While the molecular mechanism of RCR has been described, the structural mechanism is desperately lacking. Circular-rep encoded single stranded DNA (CRESS-DNA) viruses employ a viral encoded replicase (Rep) to initiate RCR. The recently identified prokaryotic homologues of Reps may also be responsible for initiating RCR. Reps are composed of an endonuclease, oligomerization, and ATPase domain. Recent structural studies have provided structures for all these domains such that an overall mechanism of RCR initiation can begin to be synthesized. However, structures of Rep in complex with its various DNA substrates and/or ligands are lacking. Here we provide a 3D bioinformatic review of the current structural information available for Reps. We combine an excess of 1590 sequences with experimental and predicted structural data from 22 CRESS-DNA groups to identify similarities and differences between Reps that lead to potentially important functional sites. Experimental studies of these sites may shed light on how Reps execute their functions. Furthermore, we identify Rep-substrate or Rep-ligand structures that are urgently needed to better understand the structural mechanism of RCR. |
| first_indexed | 2024-03-10T00:21:30Z |
| format | Article |
| id | doaj.art-1f8cc5505d7e41569d226fe52f249575 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T00:21:30Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-1f8cc5505d7e41569d226fe52f2495752023-11-23T15:41:09ZengMDPI AGViruses1999-49152021-12-011413710.3390/v14010037A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid HomologuesElvira Tarasova0Reza Khayat1Department of Chemistry and Biochemistry, City College of New York, New York, NY 10031, USADepartment of Chemistry and Biochemistry, City College of New York, New York, NY 10031, USARolling circle replication (RCR) is ubiquitously used by cellular and viral systems for genome and plasmid replication. While the molecular mechanism of RCR has been described, the structural mechanism is desperately lacking. Circular-rep encoded single stranded DNA (CRESS-DNA) viruses employ a viral encoded replicase (Rep) to initiate RCR. The recently identified prokaryotic homologues of Reps may also be responsible for initiating RCR. Reps are composed of an endonuclease, oligomerization, and ATPase domain. Recent structural studies have provided structures for all these domains such that an overall mechanism of RCR initiation can begin to be synthesized. However, structures of Rep in complex with its various DNA substrates and/or ligands are lacking. Here we provide a 3D bioinformatic review of the current structural information available for Reps. We combine an excess of 1590 sequences with experimental and predicted structural data from 22 CRESS-DNA groups to identify similarities and differences between Reps that lead to potentially important functional sites. Experimental studies of these sites may shed light on how Reps execute their functions. Furthermore, we identify Rep-substrate or Rep-ligand structures that are urgently needed to better understand the structural mechanism of RCR.https://www.mdpi.com/1999-4915/14/1/37CRESS-DNApCRESS-DNAreplicaserolling circle replicationstructureendonuclease |
| spellingShingle | Elvira Tarasova Reza Khayat A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues Viruses CRESS-DNA pCRESS-DNA replicase rolling circle replication structure endonuclease |
| title | A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues |
| title_full | A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues |
| title_fullStr | A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues |
| title_full_unstemmed | A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues |
| title_short | A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues |
| title_sort | structural perspective of reps from cress dna viruses and their bacterial plasmid homologues |
| topic | CRESS-DNA pCRESS-DNA replicase rolling circle replication structure endonuclease |
| url | https://www.mdpi.com/1999-4915/14/1/37 |
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