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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 380, Issue 10


Defining the Location and Function of Domains of McrB by Deletion Mutagenesis

Uwe Pieper / Thomas Schweitzer / Detlef H. Groll / Alfred Pingoud
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.1999.155


The GTP-dependent restriction endonuclease McrBC of E. coli K12, which recognizes cytosine-methylated DNA, consists of two protein subunits, McrB and McrC. We have investigated the structural assignment and interdependence of the McrB subunit functions, namely (i) specific DNA recognition and (ii) GTP binding and hydrolysis. Extending earlier work, we have produced McrB variants comprising N- and C-terminal fragments. The variants McrB1–162 and McrB1–170 are still capable of specific DNA binding. McrB169–465 shows GTP binding and hydrolysis characteristics indistinguishable from full-length McrB as well as wild-type like interaction with McrC. Thus, DNA and GTP binding are spatially separated on the McrB molecule, and the respective domains function quite independently.

About the article

Published Online: 2005-06-01

Published in Print: 1999-10-12

Citation Information: Biological Chemistry, Volume 380, Issue 10, Pages 1225–1230, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.1999.155.

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