The Iron-containing Domain Is Essential in Rad3 Helicases for Coupling of ATP Hydrolysis to DNA Translocation and for Targeting the Helicase to the Single-stranded DNA-Double-stranded DNA Junction-Reference-Cited by-同舟云学术

The Iron-containing Domain Is Essential in Rad3 Helicases for Coupling of ATP Hydrolysis to DNA Translocation and for Targeting the Helicase to the Single-stranded DNA-Double-stranded DNA Junction

Published:2008-01 Issue:3 Volume:283 Page:1732-1743
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pugh Robert A.,Honda Masayoshi,Leesley Haley,Thomas Alvin,Lin Yuyen,Nilges Mark J.,Cann Isaac K.O.,Spies Maria

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. Unwinding the ‘Gordian knot’ of helicase action

2. Prokaryotic and eukaryotic DNA helicases. Essential molecular motor proteins for cellular machinery

3. Helicases: amino acid sequence comparisons and structure-function relationships

4. Structure and Mechanism of Helicases and Nucleic Acid Translocases

5. Escherichia colidinG gene encodes a putative DNA helicase related to a group of eukaryotic helicases including Rad3 protein

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