The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- A Savchenko
- N Krogan
- JR Cort
- E Evdokimova
- JM Lew
- AA Yee
- L Sánchez-Pulido
- MA Andrade
- A Bochkarev
- JD Watson
- MA Kennedy
- J Greenblatt
- T Hughes
- CH Arrowsmith
- JM Rommens
- AM Edwards
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000228932300078&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1074/jbc.M414421200
- eISSN
- 1083-351X
- Externe Identifier
- Clarivate Analytics Document Solution ID: 923TN
- PubMed Identifier: 15701634
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 19
- Zeitschrift
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Paginierung
- 19213 - 19220
- Datum der Veröffentlichung
- 2005
- Status
- Published
- Titel
- The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism
- Sub types
- Article
- Ausgabe der Zeitschrift
- 280
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Alexei Savchenko
- Nevan Krogan
- John R Cort
- Elena Evdokimova
- Jocelyne M Lew
- Adelinda A Yee
- Luis Sánchez-Pulido
- Miguel A Andrade
- Alexey Bochkarev
- James D Watson
- Michael A Kennedy
- Jack Greenblatt
- Timothy Hughes
- Cheryl H Arrowsmith
- Johanna M Rommens
- Aled M Edwards
- DOI
- 10.1074/jbc.m414421200
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 19
- Zeitschrift
- Journal of Biological Chemistry
- Sprache
- en
- Paginierung
- 19213 - 19220
- Datum der Veröffentlichung
- 2005
- Status
- Published
- Herausgeber
- Elsevier BV
- Herausgeber URL
- http://dx.doi.org/10.1074/jbc.m414421200
- Datum der Datenerfassung
- 2022
- Titel
- The Shwachman-Bodian-Diamond Syndrome Protein Family Is Involved in RNA Metabolism
- Ausgabe der Zeitschrift
- 280
Datenquelle: Crossref
- Abstract
- A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold. The central domain has the common winged helix-turn-helix motif, and the C-terminal domain shares structural homology with known RNA-binding domains. Proteomic analysis of the SBDS sequence homologue in Saccharomyces cerevisiae, YLR022C, revealed an association with over 20 proteins involved in ribosome biosynthesis. NMR structural genomics revealed another yeast protein, YHR087W, to be a structural homologue of the AF0491 N-terminal domain. Sequence analysis confirmed them as distant sequence homologues, therefore related by divergent evolution. Synthetic genetic array analysis of YHR087W revealed genetic interactions with proteins involved in RNA and rRNA processing including Mdm20/Nat3, Nsr1, and Npl3. Our observations, taken together with previous reports, support the conclusion that SBDS and its homologues play a role in RNA metabolism.
- Addresses
- Ontario Center for Structural Proteomics, University of Toronto, Canada.
- Autoren
- Alexei Savchenko
- Nevan Krogan
- John R Cort
- Elena Evdokimova
- Jocelyne M Lew
- Adelinda A Yee
- Luis Sánchez-Pulido
- Miguel A Andrade
- Alexey Bochkarev
- James D Watson
- Michael A Kennedy
- Jack Greenblatt
- Timothy Hughes
- Cheryl H Arrowsmith
- Johanna M Rommens
- Aled M Edwards
- DOI
- 10.1074/jbc.m414421200
- eISSN
- 1083-351X
- Externe Identifier
- PubMed Identifier: 15701634
- Funding acknowledgements
- NIGMS NIH HHS: P50-GM62414
- NIGMS NIH HHS: P50-GM62413-02
- Open access
- false
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 19
- Zeitschrift
- The Journal of biological chemistry
- Schlüsselwörter
- Saccharomyces cerevisiae
- Archaeoglobus fulgidus
- Acetyltransferases
- Proteins
- RNA-Binding Proteins
- Saccharomyces cerevisiae Proteins
- Nuclear Proteins
- RNA
- RNA, Ribosomal
- Crystallography, X-Ray
- Magnetic Resonance Spectroscopy
- Proteomics
- Genomics
- Phylogeny
- Amino Acid Sequence
- Amino Acid Motifs
- Protein Conformation
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Protein Binding
- Protein Folding
- Sequence Homology, Amino Acid
- Molecular Sequence Data
- Static Electricity
- N-Terminal Acetyltransferase B
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2005
- Paginierung
- 19213 - 19220
- Datum der Veröffentlichung
- 2005
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2005
- Titel
- The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism.
- Sub types
- Research Support, U.S. Gov't, P.H.S.
- Research Support, Non-U.S. Gov't
- Journal Article
- Research Support, N.I.H., Extramural
- Ausgabe der Zeitschrift
- 280
Datenquelle: Europe PubMed Central
- Abstract
- A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold. The central domain has the common winged helix-turn-helix motif, and the C-terminal domain shares structural homology with known RNA-binding domains. Proteomic analysis of the SBDS sequence homologue in Saccharomyces cerevisiae, YLR022C, revealed an association with over 20 proteins involved in ribosome biosynthesis. NMR structural genomics revealed another yeast protein, YHR087W, to be a structural homologue of the AF0491 N-terminal domain. Sequence analysis confirmed them as distant sequence homologues, therefore related by divergent evolution. Synthetic genetic array analysis of YHR087W revealed genetic interactions with proteins involved in RNA and rRNA processing including Mdm20/Nat3, Nsr1, and Npl3. Our observations, taken together with previous reports, support the conclusion that SBDS and its homologues play a role in RNA metabolism.
- Autoren
- Alexei Savchenko
- Nevan Krogan
- John R Cort
- Elena Evdokimova
- Jocelyne M Lew
- Adelinda A Yee
- Luis Sánchez-Pulido
- Miguel A Andrade
- Alexey Bochkarev
- James D Watson
- Michael A Kennedy
- Jack Greenblatt
- Timothy Hughes
- Cheryl H Arrowsmith
- Johanna M Rommens
- Aled M Edwards
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/15701634
- DOI
- 10.1074/jbc.M414421200
- Funding acknowledgements
- NIGMS NIH HHS: P50-GM62413-02
- NIGMS NIH HHS: P50-GM62414
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 19
- Zeitschrift
- J Biol Chem
- Schlüsselwörter
- Acetyltransferases
- Amino Acid Motifs
- Amino Acid Sequence
- Archaeoglobus fulgidus
- Crystallography, X-Ray
- Genomics
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- N-Terminal Acetyltransferase B
- Nuclear Proteins
- Phylogeny
- Protein Binding
- Protein Conformation
- Protein Folding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Proteins
- Proteomics
- RNA
- RNA, Ribosomal
- RNA-Binding Proteins
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Sequence Homology, Amino Acid
- Static Electricity
- Sprache
- eng
- Country
- United States
- Paginierung
- 19213 - 19220
- PII
- S0021-9258(20)67571-8
- Datum der Veröffentlichung
- 2005
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2005
- Titel
- The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism.
- Sub types
- Journal Article
- Research Support, N.I.H., Extramural
- Research Support, Non-U.S. Gov't
- Research Support, U.S. Gov't, P.H.S.
- Ausgabe der Zeitschrift
- 280
Datenquelle: PubMed
- Beziehungen:
- Eigentum von