Author's Correction for Hou et al., J. Bacteriol. 190 (14) 4880-4887.
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Hou, J. M.
Right arrow Articles by Teschke, C. M.
PubMed
Right arrow Articles by Hou, J. M.
Right arrow Articles by Teschke, C. M.

 Previous Article

Journal of Bacteriology, June 2009, p. 4051, Vol. 191, No. 12
0021-9193/09/$08.00+0     doi:10.1128/JB.00468-09

AUTHOR'S CORRECTION

ATPase Activity of Mycobacterium tuberculosis SecA1 and SecA2 Proteins and Its Importance for SecA2 Function in Macrophages

Jie M. Hou, Nadia G. D'Lima, Nathan W. Rigel, Henry S. Gibbons, Jessica R. McCann, Miriam Braunstein, and Carolyn M. Teschke

Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269-3125, and Department of Microbiology and Immunology, School of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7290

Volume 190, no. 14, p. 4880-4887, 2008.

We have discovered the existence of a minor contaminating protein in our preparations of Mycobacterium tuberculosis SecA1 and SecA2 proteins. This minor contaminant is an acetate-stimulated ATPase, which we were able to remove from our protein preparations by the addition of a Q-Sepharose column. The affinity of M. tuberculosis wild-type SecA1, wild-type SecA2, and SecA2 K115R for ATP did not change after the additional purification step. The ATPase activity for M. tuberculosis SecA2 is significantly lower than first reported, and the substitution K115R in SecA2 essentially eliminates the ATPase activity. Nevertheless, the central conclusions of the paper are unchanged.

The contaminating ATPase influenced the results of the ATPase assays shown in Fig. 3B and 4C. In the figure below, panel A shows an SDS gel of a representative purification of SecA2 K115R before (lane 1) and after (lane 2) additional purification with the Q-Sepharose column. Panel B shows ATP hydrolysis with time of the SecA2 K115R variant before the Q-Sepharose column in the presence of magnesium acetate (circles) and after the Q-Sepharose column with magnesium acetate (diamonds) and magnesium chloride (squares). The ATPase activity of the proteins was determined by quantifying the amount of inorganic phosphate released from {gamma}-32P-labeled ATP with time. These data verify that the acetate-stimulated ATPase was eliminated from our protein. In panel C, the ATP hydrolysis rates of Escherichia coli SecA and Q-Sepharose-purified M. tuberculosis SecA1, SecA2, and SecA2 K115R proteins are shown with 5 mM magnesium chloride used in the reaction buffer.


Figure 1
View larger version (28K):
[in this window]
[in a new window]

 

Journal of Bacteriology, June 2009, p. 4051, Vol. 191, No. 12
0021-9193/09/$08.00+0     doi:10.1128/JB.00468-09





This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Hou, J. M.
Right arrow Articles by Teschke, C. M.
PubMed
Right arrow Articles by Hou, J. M.
Right arrow Articles by Teschke, C. M.

Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»