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Journal of Bacteriology, February 2005, p. 1188-1191, Vol. 187, No. 3
0021-9193/05/$08.00+0     doi:10.1128/JB.187.3.1188-1191.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Site-Directed Mutagenesis Analysis of Amino Acids Critical for Activity of the Type I Signal Peptidase of the Archaeon Methanococcus voltae

Sonia L. Bardy,^1, Sandy Y. M. Ng,^1, David S. Carnegie,¹ and Ken F. Jarrell^1*

Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada¹

Received 19 August 2004/ Accepted 29 October 2004

Site-directed mutagenesis studies of the signal peptidase of the methanogenic archaeon Methanococcus voltae identified three conserved residues (Ser⁵², His¹²², and Asp¹⁴⁸) critical for activity. The requirement for one conserved aspartic acid residue distinguishes the archaeal enzyme from both the Escherichia coli and yeast Sec11 enzymes.

S.L.B. and S.Y.M.N. contributed equally to the work reported.

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