Structure-Based Stability Analysis of an Extremely Stable Dimeric DNA Binding Protein from Sulfolobus islandicus-Reference-Cited by-同舟云学术

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Structure-Based Stability Analysis of an Extremely Stable Dimeric DNA Binding Protein from Sulfolobus islandicus

Published:2009-09-29 Issue:42 Volume:48 Page:10030-10037
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Weininger Ulrich¹²,Zeeb Markus³,Neumann Piotr⁴,Löw Christian¹,Stubbs Milton T.²⁴,Lipps Georg³,Balbach Jochen¹²

Affiliation:

1. Institut für Physik, Biophysik, Martin-Luther-Universität Halle-Wittenberg, D-06120 Halle (Saale), Germany

2. Mitteldeutsches Zentrum für Struktur und Dynamik der Proteine (MZP), Martin-Luther-Universität Halle-Wittenberg, D-06120 Halle (Saale), Germany

3. Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany

4. Institut für Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, D-06120 Halle (Saale), Germany.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi900760n

Reference52 articles.

1. Evolution of the family of pRN plasmids and their integrase-mediated insertion into the chromosome of the crenarchaeon Sulfolobus solfataricus 1 1Edited by J. Karn

2. Plasmids and viruses of the thermoacidophilic crenarchaeote Sulfolobus

3. The protein ORF80 from the acidophilic and thermophilic archaeon Sulfolobus islandicus binds highly site-specifically to double-stranded DNA and represents a novel type of basic leucine zipper protein

4. A novel type of replicative enzyme harbouring ATPase, primase and DNA polymerase activity

5. Structure of a bifunctional DNA primase-polymerase

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