Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor
Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solut...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2013-09, Vol.110 (39), p.15656-15661 |
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| creator | Simonetti, Angelita Marzi, Stefano Billas, Isabelle M. L. Tsai, Albert Fabbretti, Attilio Myasnikov, Alexander G. Roblin, Pierre Vaiana, Andrea C. Hazemann, Isabelle Eiler, Daniel Steitz, Thomas A. Puglisi, Joseph D. Gualerzi, Claudio O. Klaholz, Bruno P. |
| description | Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl (fMet)-tRNA fMet positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. Together, our data highlight the dynamics of IF2-dependent ribosomal subunit joining and the role played by the N terminus of IF2 in this process. |
| doi_str_mv | 10.1073/pnas.1309578110 |
| format | Article |
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L. ; Tsai, Albert ; Fabbretti, Attilio ; Myasnikov, Alexander G. ; Roblin, Pierre ; Vaiana, Andrea C. ; Hazemann, Isabelle ; Eiler, Daniel ; Steitz, Thomas A. ; Puglisi, Joseph D. ; Gualerzi, Claudio O. ; Klaholz, Bruno P.</creator><creatorcontrib>Simonetti, Angelita ; Marzi, Stefano ; Billas, Isabelle M. L. ; Tsai, Albert ; Fabbretti, Attilio ; Myasnikov, Alexander G. ; Roblin, Pierre ; Vaiana, Andrea C. ; Hazemann, Isabelle ; Eiler, Daniel ; Steitz, Thomas A. ; Puglisi, Joseph D. ; Gualerzi, Claudio O. ; Klaholz, Bruno P.</creatorcontrib><description>Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl (fMet)-tRNA fMet positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. 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L.</creatorcontrib><creatorcontrib>Tsai, Albert</creatorcontrib><creatorcontrib>Fabbretti, Attilio</creatorcontrib><creatorcontrib>Myasnikov, Alexander G.</creatorcontrib><creatorcontrib>Roblin, Pierre</creatorcontrib><creatorcontrib>Vaiana, Andrea C.</creatorcontrib><creatorcontrib>Hazemann, Isabelle</creatorcontrib><creatorcontrib>Eiler, Daniel</creatorcontrib><creatorcontrib>Steitz, Thomas A.</creatorcontrib><creatorcontrib>Puglisi, Joseph D.</creatorcontrib><creatorcontrib>Gualerzi, Claudio O.</creatorcontrib><creatorcontrib>Klaholz, Bruno P.</creatorcontrib><title>Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl (fMet)-tRNA fMet positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. Together, our data highlight the dynamics of IF2-dependent ribosomal subunit joining and the role played by the N terminus of IF2 in this process.</description><subject>Architecture</subject><subject>Biological Sciences</subject><subject>Biology</subject><subject>Chemical and Process Engineering</subject><subject>cryo-electron microscopy</subject><subject>Cryoelectron Microscopy</subject><subject>Crystal structure</subject><subject>Diffraction</subject><subject>Engineering Sciences</subject><subject>Escherichia coli</subject><subject>Fluorescence</subject><subject>Food engineering</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Mathematical functions</subject><subject>Models, Molecular</subject><subject>Molecular structure</subject><subject>Molecules</subject><subject>Mutant Proteins - metabolism</subject><subject>Peptide Chain Initiation, Translational</subject><subject>Peptide initiation factors</subject><subject>Prokaryotic Initiation Factor-2 - chemistry</subject><subject>Prokaryotic Initiation Factor-2 - metabolism</subject><subject>Prokaryotic Initiation Factor-2 - ultrastructure</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>protein subunits</subject><subject>Proteins</subject><subject>Ribonucleic acid</subject><subject>ribosomal proteins</subject><subject>Ribosome Subunits - metabolism</subject><subject>Ribosome Subunits, Large, Bacterial</subject><subject>Ribosome Subunits, Small, Bacterial</subject><subject>Ribosomes</subject><subject>RNA</subject><subject>Sampling</subject><subject>Scattering, Small Angle</subject><subject>Structure-Activity Relationship</subject><subject>Thermus thermophilus - metabolism</subject><subject>X-Ray Diffraction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFksGO0zAQhiMEYsvCmRPIEhc4ZHdsJ7FzQVqtWLZSBRc4W64zaV0ldrGdSjwE74xDS4G9IFmyZuabf8bjKYqXFK4oCH69dzpeUQ5tLSSl8KhYUGhp2VQtPC4WAEyUsmLVRfEsxh1A5iQ8LS5YBawFKhbFj6U7-OGAI7pEfE_2wSe0jizvGPlEOj_qbOQT7NrHbA0kTuvJ2UR23jrrNiTgAfWAHemDH4kOZmsTmjQFJNpl7-RMst7N4mmL2R6GckC3Sdusa5PVv6K9NsmH58WTXg8RX5zuy-Lr3Ycvt_fl6vPH5e3NqjQN0FRys0YpeokNp32v604AVLKWaNa9MRX23BjArqfYCqZN3UnsDG1BtMBbSgW_LN4fdffTesyx_PigB7UPdtThu_Laqn8jzm7Vxh8UF7IWArLAu6PA9kHa_c1KzT5gTVWDrA80s29PxYL_NmFMarTR4DBoh36KikrglDYViP-jFRe5_5qzjL55gO78FFye2kxJ2VLGmkxdHykTfIwB-3OzFNS8QWreIPVng3LG679Hc-Z_r0wGyAmYM89yWY-3itZNPVd9dUR2MX_qmamYoJznP_gJDsPYPg</recordid><startdate>20130924</startdate><enddate>20130924</enddate><creator>Simonetti, Angelita</creator><creator>Marzi, Stefano</creator><creator>Billas, Isabelle M. 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L. ; Tsai, Albert ; Fabbretti, Attilio ; Myasnikov, Alexander G. ; Roblin, Pierre ; Vaiana, Andrea C. ; Hazemann, Isabelle ; Eiler, Daniel ; Steitz, Thomas A. ; Puglisi, Joseph D. ; Gualerzi, Claudio O. ; Klaholz, Bruno P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c601t-3cbe87f8e631ffa5d7004858ecbfcc4ef3cc0edf1e972ac5d8edc190790391173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Architecture</topic><topic>Biological Sciences</topic><topic>Biology</topic><topic>Chemical and Process Engineering</topic><topic>cryo-electron microscopy</topic><topic>Cryoelectron Microscopy</topic><topic>Crystal structure</topic><topic>Diffraction</topic><topic>Engineering Sciences</topic><topic>Escherichia coli</topic><topic>Fluorescence</topic><topic>Food engineering</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Mathematical functions</topic><topic>Models, Molecular</topic><topic>Molecular structure</topic><topic>Molecules</topic><topic>Mutant Proteins - metabolism</topic><topic>Peptide Chain Initiation, Translational</topic><topic>Peptide initiation factors</topic><topic>Prokaryotic Initiation Factor-2 - chemistry</topic><topic>Prokaryotic Initiation Factor-2 - metabolism</topic><topic>Prokaryotic Initiation Factor-2 - ultrastructure</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>protein subunits</topic><topic>Proteins</topic><topic>Ribonucleic acid</topic><topic>ribosomal proteins</topic><topic>Ribosome Subunits - metabolism</topic><topic>Ribosome Subunits, Large, Bacterial</topic><topic>Ribosome Subunits, Small, Bacterial</topic><topic>Ribosomes</topic><topic>RNA</topic><topic>Sampling</topic><topic>Scattering, Small Angle</topic><topic>Structure-Activity Relationship</topic><topic>Thermus thermophilus - metabolism</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Simonetti, Angelita</creatorcontrib><creatorcontrib>Marzi, Stefano</creatorcontrib><creatorcontrib>Billas, Isabelle M. 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L.</au><au>Tsai, Albert</au><au>Fabbretti, Attilio</au><au>Myasnikov, Alexander G.</au><au>Roblin, Pierre</au><au>Vaiana, Andrea C.</au><au>Hazemann, Isabelle</au><au>Eiler, Daniel</au><au>Steitz, Thomas A.</au><au>Puglisi, Joseph D.</au><au>Gualerzi, Claudio O.</au><au>Klaholz, Bruno P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2013-09-24</date><risdate>2013</risdate><volume>110</volume><issue>39</issue><spage>15656</spage><epage>15661</epage><pages>15656-15661</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl (fMet)-tRNA fMet positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. Together, our data highlight the dynamics of IF2-dependent ribosomal subunit joining and the role played by the N terminus of IF2 in this process.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>24029017</pmid><doi>10.1073/pnas.1309578110</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0003-0399-4613</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Architecture Biological Sciences Biology Chemical and Process Engineering cryo-electron microscopy Cryoelectron Microscopy Crystal structure Diffraction Engineering Sciences Escherichia coli Fluorescence Food engineering Kinetics Life Sciences Mathematical functions Models, Molecular Molecular structure Molecules Mutant Proteins - metabolism Peptide Chain Initiation, Translational Peptide initiation factors Prokaryotic Initiation Factor-2 - chemistry Prokaryotic Initiation Factor-2 - metabolism Prokaryotic Initiation Factor-2 - ultrastructure Protein Binding Protein Structure, Tertiary protein subunits Proteins Ribonucleic acid ribosomal proteins Ribosome Subunits - metabolism Ribosome Subunits, Large, Bacterial Ribosome Subunits, Small, Bacterial Ribosomes RNA Sampling Scattering, Small Angle Structure-Activity Relationship Thermus thermophilus - metabolism X-Ray Diffraction |
| title | Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor |
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