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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-2-7
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pubmed:databankReference |
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pubmed:abstractText |
We determined a 1.95 A X-ray crystal structure of a C-terminally truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions in splicing group I introns. CYT-18's nucleotide binding fold and intermediate alpha-helical domains superimpose on those of bacterial TyrRSs, except for an N-terminal extension and two small insertions not found in nonsplicing bacterial enzymes. These additions surround the cyt-18-1 mutation site and are sites of suppressor mutations that restore splicing, but not synthetase activity. Highly constrained models based on directed hydroxyl radical cleavage assays show that the group I intron binds at a site formed in part by the three additions on the nucleotide binding fold surface opposite that which binds tRNATyr. Our results show how essential proteins can progressively evolve new functions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
417-28
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15694342-Amino Acid Sequence,
pubmed-meshheading:15694342-Amino Acid Substitution,
pubmed-meshheading:15694342-Catalytic Domain,
pubmed-meshheading:15694342-Crystallography, X-Ray,
pubmed-meshheading:15694342-Genes, Fungal,
pubmed-meshheading:15694342-Hydroxyl Radical,
pubmed-meshheading:15694342-Introns,
pubmed-meshheading:15694342-Models, Molecular,
pubmed-meshheading:15694342-Molecular Sequence Data,
pubmed-meshheading:15694342-Mutagenesis, Insertional,
pubmed-meshheading:15694342-Mutagenesis, Site-Directed,
pubmed-meshheading:15694342-Neurospora crassa,
pubmed-meshheading:15694342-Nucleic Acid Conformation,
pubmed-meshheading:15694342-Protein Structure, Tertiary,
pubmed-meshheading:15694342-RNA, Fungal,
pubmed-meshheading:15694342-RNA, Transfer, Amino Acyl,
pubmed-meshheading:15694342-RNA Splicing,
pubmed-meshheading:15694342-Sequence Homology, Amino Acid,
pubmed-meshheading:15694342-Static Electricity,
pubmed-meshheading:15694342-Tyrosine-tRNA Ligase
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pubmed:year |
2005
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pubmed:articleTitle |
A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface.
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pubmed:affiliation |
Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry and Section of Molecular Genetics and Microbiology, School of Biological Sciences, University of Texas, Austin, TX 78712, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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