Structural and Functional Studies of RegB, a New Member of a Family of Sequence-specific Ribonucleases Involved in mRNA Inactivation on the Ribosome
The RegB endoribonuclease participates in the bacteriophage T4 life cycle by favoring early messenger RNA breakdown. RegB specifically cleaves GGAG sequences found in intergenic regions, mainly in translation initiation sites. Its activity is very low but can be enhanced up to 100-fold by the riboso...
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| Veröffentlicht in: | The Journal of biological chemistry 2007-01, Vol.282 (3), p.2019-2028 |
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| container_issue | 3 |
| container_start_page | 2019 |
| container_title | The Journal of biological chemistry |
| container_volume | 282 |
| creator | Odaert, Benoît Saïda, Fakhri Aliprandi, Pascale Durand, Sylvain Créchet, Jean-Bernard Guerois, Raphaël Laalami, Soumaya Uzan, Marc Bontems, François |
| description | The RegB endoribonuclease participates in the bacteriophage T4 life cycle by favoring early messenger RNA breakdown. RegB specifically cleaves GGAG sequences found in intergenic regions, mainly in translation initiation sites. Its activity is very low but can be enhanced up to 100-fold by the ribosomal 30 S subunit or by ribosomal protein S1. RegB has no significant sequence homology to any known protein. Here we used NMR to solve the structure of RegB and map its interactions with two RNA substrates. We also generated a collection of mutants affected in RegB function. Our results show that, despite the absence of any sequence homology, RegB has structural similarities with two Escherichia coli ribonucleases involved in mRNA inactivation on translating ribosomes: YoeB and RelE. Although these ribonucleases have different catalytic sites, we propose that RegB is a new member of the RelE/YoeB structural and functional family of ribonucleases specialized in mRNA inactivation within the ribosome. |
| doi_str_mv | 10.1074/jbc.M608271200 |
| format | Article |
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RegB specifically cleaves GGAG sequences found in intergenic regions, mainly in translation initiation sites. Its activity is very low but can be enhanced up to 100-fold by the ribosomal 30 S subunit or by ribosomal protein S1. RegB has no significant sequence homology to any known protein. Here we used NMR to solve the structure of RegB and map its interactions with two RNA substrates. We also generated a collection of mutants affected in RegB function. Our results show that, despite the absence of any sequence homology, RegB has structural similarities with two Escherichia coli ribonucleases involved in mRNA inactivation on translating ribosomes: YoeB and RelE. Although these ribonucleases have different catalytic sites, we propose that RegB is a new member of the RelE/YoeB structural and functional family of ribonucleases specialized in mRNA inactivation within the ribosome.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M608271200</identifier><identifier>PMID: 17046813</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Bacterial Toxins - metabolism ; Bacteriophage T4 - metabolism ; Biochemistry, Molecular Biology ; Catalytic Domain ; Escherichia coli ; Escherichia coli - metabolism ; Escherichia coli Proteins - metabolism ; Life Sciences ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Biosynthesis ; Protein Conformation ; Ribonucleases - biosynthesis ; Ribonucleases - chemistry ; Ribosomes - metabolism ; RNA, Messenger - metabolism</subject><ispartof>The Journal of biological chemistry, 2007-01, Vol.282 (3), p.2019-2028</ispartof><rights>2007 © 2007 ASBMB. 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RegB specifically cleaves GGAG sequences found in intergenic regions, mainly in translation initiation sites. Its activity is very low but can be enhanced up to 100-fold by the ribosomal 30 S subunit or by ribosomal protein S1. RegB has no significant sequence homology to any known protein. Here we used NMR to solve the structure of RegB and map its interactions with two RNA substrates. We also generated a collection of mutants affected in RegB function. Our results show that, despite the absence of any sequence homology, RegB has structural similarities with two Escherichia coli ribonucleases involved in mRNA inactivation on translating ribosomes: YoeB and RelE. Although these ribonucleases have different catalytic sites, we propose that RegB is a new member of the RelE/YoeB structural and functional family of ribonucleases specialized in mRNA inactivation within the ribosome.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Toxins - metabolism</subject><subject>Bacteriophage T4 - metabolism</subject><subject>Biochemistry, Molecular Biology</subject><subject>Catalytic Domain</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Life Sciences</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Protein Biosynthesis</subject><subject>Protein Conformation</subject><subject>Ribonucleases - biosynthesis</subject><subject>Ribonucleases - chemistry</subject><subject>Ribosomes - metabolism</subject><subject>RNA, Messenger - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU1v1DAQhiMEokvhyhEsDkhIZLGdD9vHpWJppW2RdqnEzXKc8a6rJN7aSar-D34wDlnRE5Yl2-Nn3hn7TZK3BC8JZvmXu0ovr0vMKSMU42fJgmCepVlBfj1PFhhTkgpa8LPkVQh3OI5ckJfJGWE4LznJFsnvXe8H3Q9eNUh1NVoPne6t6-Jx1w-1hYCcQVvYf_2MFLqBB3QNbQV-iiq0Vq1tHqf9Du4H6DSk4QjaGqvR1lauG3QDKkSRq250zQg1sh1qtzerGFCx0KimYijO_gB_U4Jr4XXywqgmwJvTep7crr_9vLhMNz--X12sNqkuyrxPGeY540xQLGplKGfUZERwkme8FMxwUwKrRM1zg_NcxX8oTUlIXtSVYlkh6uw8-TTrHlQjj962yj9Kp6y8XG3kFMOYEMIoH0lkP87s0bv41NDL1gYNTaM6cEOQFJeiJJxHcDmD2rsQPJh_ygTLyTMZPZNPnsWEdyfloWqhfsJPJkXgw6lNuz88WA-ysk4foJWUU5nF0kRE6P0MGeWk2nsb5O0u3mQYs6wUxdQYnwmIXzpa8DJoO3lWR0ndy9rZ_7X4ByjGuB4</recordid><startdate>20070119</startdate><enddate>20070119</enddate><creator>Odaert, Benoît</creator><creator>Saïda, Fakhri</creator><creator>Aliprandi, Pascale</creator><creator>Durand, Sylvain</creator><creator>Créchet, Jean-Bernard</creator><creator>Guerois, Raphaël</creator><creator>Laalami, Soumaya</creator><creator>Uzan, Marc</creator><creator>Bontems, François</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0001-5294-2858</orcidid><orcidid>https://orcid.org/0000-0003-3509-6463</orcidid><orcidid>https://orcid.org/0000-0002-4166-4845</orcidid></search><sort><creationdate>20070119</creationdate><title>Structural and Functional Studies of RegB, a New Member of a Family of Sequence-specific Ribonucleases Involved in mRNA Inactivation on the Ribosome</title><author>Odaert, Benoît ; 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| subjects | Amino Acid Sequence Bacterial Toxins - metabolism Bacteriophage T4 - metabolism Biochemistry, Molecular Biology Catalytic Domain Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins - metabolism Life Sciences Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Protein Biosynthesis Protein Conformation Ribonucleases - biosynthesis Ribonucleases - chemistry Ribosomes - metabolism RNA, Messenger - metabolism |
| title | Structural and Functional Studies of RegB, a New Member of a Family of Sequence-specific Ribonucleases Involved in mRNA Inactivation on the Ribosome |
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