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ID: 16645.0, MPI für biophysikalische Chemie / Abteilungsunabhängige Arbeitsgruppen
Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities
Authors:Steiner, T.; Kaiser, J. T.; Marinkovic, S.; Huber, R.; Wahl, M. C.
Language:English
Date of Publication (YYYY-MM-DD):2002-09-02
Title of Journal:EMBO Journal
Volume:21
Issue / Number:17
Start Page:4641
End Page:4653
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Microbial transcription modulator NusG interacts with RNA polymerase and termination factor rho, displaying striking functional homology to eukaryotic Spt5. The protein is also a translational regulator. We have determined crystal structures of Aquifex aeolicus NusG showing a modular design: an N- terminal RNP-like domain, a C-terminal element with a KOW sequence motif and a species-specific immunoglobulin-like fold. The structures reveal bona fide nucleic acid binding sites, and nucleic acid binding activities can be detected for NusG from three organisms and for the KOW element alone. A conserved KOW domain is defined as a new class of nucleic acid binding folds. This module is a close structural homolog of tudor protein- protein interaction motifs. Putative protein binding sites for the RNP and KOW domains can be deduced, which differ from the areas implicated in nucleic acid interactions. The results strongly argue that both protein and nucleic acid contacts are important for NusG's functions and that the factor can act as an adaptor mediating indirect protein-nucleic acid associations.
Free Keywords:KOW domain; NusG; protein-nucleic acid interaction; regulation of transcription and translation; transcription termination and antitermination
Comment of the Author/Creator:Date: 2002, SEP 2
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/AG Markus Wahl
External Affiliations:Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany
Identifiers:URL:http://www.nature.com/emboj/journal/v21/n17/pdf/75...
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