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  Functions of DNA Helicases in the DNA Metabolism of Escherichia Coli

Abdel-Monem, M., Arthur, H. M., Benz, I., Hoffmann-Berling, H., Reygers, U., Seiter, A., et al. (1984). Functions of DNA Helicases in the DNA Metabolism of Escherichia Coli. Proteins Involved in DNA Replication, 385-393. doi:10.1007/978-1-4684-8730-5_40.

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ProteinsAndNucleotideSequences_1984_385.pdf (Any fulltext), 846KB
 
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Abdel-Monem, Mahmoud1, Author           
Arthur , Helen M., Author
Benz, Inga1, Author           
Hoffmann-Berling, Hartmut2, Author           
Reygers, Ursula1, Author           
Seiter, Anita, Author
Taucher-Scholz, Gisela1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Department of Molecular Biology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497702              

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Free keywords: Replication Fork, Chromosomal Replication, Chemical Polarity, Single Strand Binding Protein, Helicase Protein
 Abstract: DNA helicases catalyze the separation of double-stranded DNA into single strands using the energy of ATP hydrolysis. The four helicases which have been found in Escherichia coli are listed in Table 1. These enzymes are the helicases I, II, III and the helicase specified by the rep gene. As the table shows the four proteins differ considerably with respect to Mr, number of molecules per cell and, in particular, mechanism of action. Each of the helicases requires a region of single-stranded DNA to initiate unwinding, and each of the four enzymes unwinds DNA unidirectionally relative to the chemical polarity of the DNA strand to which it is bound. The direction of unwinding depends on the nature of the helicase.

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Language(s): eng - English
 Dates: 1984
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-1-4684-8730-5_40
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Title: Proteins Involved in DNA Replication
Source Genre: Journal
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Publ. Info: New York [u.a.] : Springer
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 385 - 393 Identifier: ISBN: 978-1-4684-8730-5
ISBN: 978-1-4684-8732-9