RNA polymerase subunit H features a β-ribbon motif within a novel fold that is present in archaea and eukaryotes
The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon Methanococcus jannaschii using multidimensional nuclea...
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| Published in: | Journal of molecular biology Vol. 287; no. 4; pp. 753 - 760 |
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| Main Authors: | , , , , , |
| Format: | Journal Article |
| Language: | English |
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Elsevier Ltd
09-04-1999
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| Abstract | The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon
Methanococcus jannaschii using multidimensional nuclear magnetic resonance. The structure reveals a novel fold containing a four-stranded mixed β sheet that is flanked on one side by three short helices. The dominant feature is β-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold. |
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| AbstractList | The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon Methanococcus jannaschii using multidimensional nuclear magnetic resonance. The structure reveals a novel fold containing a four-stranded mixed beta sheet that is flanked on one side by three short helices. The dominant feature is beta-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold. The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from archaea to humans. We report the structure of subunit H, in solution, from the archaeon Methanococcus jannaschii using multidimensional nuclear magnetic resonance. The structure reveals a novel fold containing a four-stranded mixed β sheet that is flanked on one side by three short helices. The dominant feature is β-ribbon motif, which presents a hydrophobic, basic surface, and defines a general RNA polymerase architectural scaffold. |
| Author | Weinzierl, Robert O.J Eloranta, Jyrki J Thiru, Abarna Hodach, Meri Matthews, Stephen Kostourou, Vassiliki |
| Author_xml | – sequence: 1 givenname: Abarna surname: Thiru fullname: Thiru, Abarna organization: Department of Biochemistry Imperial College of Science Technology and Medicine Exhibition Road, South Kensington, London SW7 2AY UK – sequence: 2 givenname: Meri surname: Hodach fullname: Hodach, Meri organization: Department of Biochemistry Imperial College of Science Technology and Medicine Exhibition Road, South Kensington, London SW7 2AY UK – sequence: 3 givenname: Jyrki J surname: Eloranta fullname: Eloranta, Jyrki J organization: Department of Biochemistry Imperial College of Science Technology and Medicine Exhibition Road, South Kensington, London SW7 2AY UK – sequence: 4 givenname: Vassiliki surname: Kostourou fullname: Kostourou, Vassiliki organization: Department of Biochemistry Imperial College of Science Technology and Medicine Exhibition Road, South Kensington, London SW7 2AY UK – sequence: 5 givenname: Robert O.J surname: Weinzierl fullname: Weinzierl, Robert O.J organization: Department of Biochemistry Imperial College of Science Technology and Medicine Exhibition Road, South Kensington, London SW7 2AY UK – sequence: 6 givenname: Stephen surname: Matthews fullname: Matthews, Stephen email: s.j.matthews@ic.ac.uk organization: Department of Biochemistry Imperial College of Science Technology and Medicine Exhibition Road, South Kensington, London SW7 2AY UK |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10191143$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1073_pnas_97_12_6306 crossref_primary_10_1016_S1369_5274_00_00190_9 crossref_primary_10_1371_journal_pone_0087485 crossref_primary_10_1016_S0969_2126_99_80093_8 crossref_primary_10_1107_S1744309111033288 crossref_primary_10_1016_S1097_2765_02_00629_9 crossref_primary_10_1073_pnas_97_12_6311 |
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| Keywords | thermostability RPB5 triple resonance NMR archaea |
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| Snippet | The archaeal H and eukaryotic RPB5 RNA polymerase subunits are highly homologous and are likely to play a fundamental role in transcription that extends from... |
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| SubjectTerms | Amino Acid Sequence archaea Base Sequence Crystallography, X-Ray DNA Primers DNA-Directed RNA Polymerases - chemistry Enzyme Stability Eukaryotic Cells - enzymology Humans Magnetic Resonance Spectroscopy Methanococcus - enzymology Methanococcus jannaschii Models, Molecular Molecular Sequence Data Protein Conformation Protein Folding Recombinant Proteins - chemistry RPB5 Sequence Homology, Amino Acid thermostability triple resonance NMR |
| Title | RNA polymerase subunit H features a β-ribbon motif within a novel fold that is present in archaea and eukaryotes |
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