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Journal of Bacteriology, January 2001, p. 528-535, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.528-535.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Involvement of the XpsN Protein in Formation of the XpsL-XpsM Complex in Xanthomonas campestris pv. campestris Type II Secretion Apparatus

Hsien-Ming Lee,1 Shiaw-Wei Tyan,2 Wei-Ming Leu,1 Ling-Yun Chen,3 David Chanhen Chen,4 and Nien-Tai Hu2,5,*

Graduate Institute of Agricultural Biotechnology,1 Graduate Institute of Biological Chemistry,2 Graduate Institute of Veterinary Microbiology,4 and Agricultural Biotechnology Laboratories,5 National Chung Hsing University, and Graduate Institute of Biochemistry, Chung Shan Medical and Dental College,3 Taichung, Taiwan, Republic of China

Received 21 June 2000/Accepted 20 October 2000

The xps gene cluster is required for the second step of type II protein secretion in Xanthomonas campestris pv. campestris. Deletion of the entire gene cluster caused accumulation of secreted proteins in the periplasm. By analyzing protein abundance in the chromosomal mutant strains, we observed mutual dependence for normal steady-state levels between the XpsL and the XpsM proteins. The XpsL protein was undetectable in total lysate prepared from the xpsM mutant strain, and vice versa. Introduction of the wild-type xpsM gene carried on a plasmid into the xpsM mutant strain was sufficient for reappearance of the XpsL protein, and vice versa. Moreover, both XpsL and XpsM proteins were undetectable in the xpsN mutant strain. They were recovered either by reintroducing the wild-type xpsN gene or by introducing extra copies of wild-type xpsL or xpsM individually. Overproduction of wild-type XpsL and -M proteins simultaneously, but not separately, in the wild-type strain of X. campestris pv. campestris caused inhibition of secretion. Complementation of an xpsL or xpsM mutant strain with a plasmid-borne wild-type gene was inhibited by coexpression of XpsL and XpsM. The presence of the xpsN gene on the plasmid along with the xpsL and the xpsM genes caused more severe inhibition in both cases. Furthermore, complementation of the xpsN mutant strain was also inhibited. In both the wild-type strain and a strain with the xps gene cluster deleted (XC17433), carrying pCPP-LMN, which encodes all three proteins, each protein coprecipitated with the other two upon immunoprecipitation. Expression of pairwise combinations of the three proteins in XC17433 revealed that the XpsL-XpsM and XpsM-XpsN pairs still coprecipitated, whereas the XpsL-XpsN pair no longer coprecipitated.

* Corresponding author. Mailing address: Graduate Institute of Biological Chemistry, National Chung Hsing University, Taichung 40227, Taiwan, Republic of China. Phone: 886-4-2874754. Fax: 886-4-2861905. E-mail: nthu{at}nchu.edu.tw.

Journal of Bacteriology, January 2001, p. 528-535, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.528-535.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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