|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 274, Issue 2, 825-832, January 8, 1999
From the Institut für Biochemie, Fachbereich Biologie,
Justus-Liebig Universität, Heinrich-Buff-Ring 58, D-35392 Giessen, Germany
The extracellular endonucleases from
Serratia marcescens and Anabaena sp. are
members of a family of nonspecific endonucleases. In contrast to the
monomeric Anabaena nuclease, the Serratia
nuclease is a dimer of two identical subunits. To find out whether the two active sites of the Serratia nuclease function
independently of each other and what the advantage of being a dimer for
this enzyme might be, we produced (i) dimers in which the two subunits were cross-linked, (ii) heterodimers consisting of a wild type and an
inactive mutant subunit which were also cross-linked, and (iii)
monomeric variants which are unable to dimerize. The monomeric H184R
variant and the cross-linked S140C variant exhibit the same activity as
the wild type enzyme, while the cross-linked heterodimer with one
inactive subunit shows only half of the activity of the wild type
enzyme, demonstrating functional independence of the two subunits of
the Serratia nuclease. On the other hand at low enzyme and
substrate concentrations dimeric forms of the Serratia nuclease are relatively more active than monomeric forms or the monomeric Anabaena nuclease in cleaving polynucleotides,
not, however, oligonucleotides, which is correlated with the ability of
dimeric forms of the Serratia nuclease to form large
enzyme-substrate networks with high molecular weight DNA and to cleave
polynucleotides in a processive manner. We conclude that in the natural
habitat of Serratia marcescens where the supply of
nutrients may become growth limiting the dimeric nuclease can fulfil
its nutritive function more efficiently than a monomeric enzyme.
On the Advantage of Being a Dimer, a Case Study Using the Dimeric
Serratia Nuclease and the Monomeric Nuclease from
Anabaena sp. Strain PCC 7120
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  C. Temme, R. Weissbach, H. Lilie, C. Wilson, A. Meinhart, S. Meyer, R. Golbik, A. Schierhorn, and E. Wahle The Drosophila melanogaster Gene cg4930 Encodes a High Affinity Inhibitor for Endonuclease G J. Biol. Chem., March 27, 2009; 284(13): 8337 - 8348. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Reh, C. Korn, O. Gimadutdinow, and G. Meiss Structural Basis for Stable DNA Complex Formation by the Caspase-activated DNase J. Biol. Chem., December 16, 2005; 280(50): 41707 - 41715. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Ghosh, G. Meiss, A. Pingoud, R. E. London, and L. C. Pedersen Structural Insights into the Mechanism of Nuclease A, a {beta}{beta}{alpha} Metal Nuclease from Anabaena J. Biol. Chem., July 29, 2005; 280(30): 27990 - 27997. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Z. Yang, J. R. Horton, R. Maunus, G. G. Wilson, R. J. Roberts, and X. Cheng Structure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI Nucleic Acids Res., April 1, 2005; 33(6): 1892 - 1901. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. M. Davies, S. Hershman, G. J. Stabley, J. B. Hoek, J. Peterson, and A. Cahill A Ca2+-induced mitochondrial permeability transition causes complete release of rat liver endonuclease G activity from its exclusive location within the mitochondrial intermembrane space. Identification of a novel endo-exonuclease activity residing within the mitochondrial matrix Nucleic Acids Res., February 15, 2003; 31(4): 1364 - 1373. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |