NDLI: Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases.

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Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases.

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Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yu, X. Hingorani, M. M. Egelman, E. H. Wild, R. Patel, S. S.
Description	Author Affiliation: Egelman EH ( Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis 55455, USA.);
Abstract	Most helicases studied to date have been characterized as oligomeric, but the relation between their structure and function has not been understood. The bacteriophage T7 gene 4 helicase/primase proteins act in T7 DNA replication. We have used electron microscopy, three-dimensional reconstruction, and protein crosslinking to demonstrate that both proteins form hexameric rings around single-stranded DNA. Each subunit has two lobes, so the hexamer appears to be two-tiered, with a small ring stacked on a large ring. The single-stranded DNA passes through the central hole of the hexamer, and the data exclude substantial wrapping of the DNA about or within the protein ring. Further, the hexamer binds DNA with a defined polarity as the smaller ring of the hexamer points toward the 5' end of the DNA. The similarity in three-dimensional structure of the T7 gene 4 proteins to that of the Escherichia coli RuvB helicase suggests that polar rings assembled around DNA may be a general feature of numerous hexameric helicases involved in DNA replication, transcription, recombination, and repair.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriophage T7 Enzymology DNA Helicases Chemistry Metabolism DNA, Single-Stranded RNA Nucleotidyltransferases Binding Sites Ultrastructure DNA Primase Macromolecular Substances Microscopy, Electron Models, Molecular Neural Networks (Computer) Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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