This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services E-mail this article to a friend Similar articles in this journal Similar articles in ASM journals Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lei, G. S. Articles by Hu, S. T. Search for Related Content PubMed PubMed Citation Articles by Lei, G. S. Articles by Hu, S. T.

 Previous Article  |  Next Article 

J. Bacteriol., Oct 1997, 6238-6243, Vol 179, No. 20
Copyright © 1997, American Society for Microbiology

Functional domains of the InsA protein of IS2

GS Lei and ST Hu
Department of Microbiology and Graduate Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan, Republic of China.

The InsA protein is a transcriptional regulator. It binds to the promoter region of insA and insAB'. To understand the molecular mechanism for the interaction between InsA and its binding sequence, the functional domains of InsA were identified. The glutaraldehyde cross-linking method and the two-hybrid expression system were used to study the protein-protein interaction of InsA. The results of these experiments showed that InsA forms homodimers. Deletion of the last 44 amino acid residues at its C terminus, but not the first 12 or 57 residues at the N terminus, abolished the ability of InsA to form homodimers, indicating that the protein-protein interaction domain of InsA is located at its C terminus. Gel retardation assays revealed that deletion of the last 29 amino acid residues at its C terminus had no effect on the DNA binding ability of InsA. In contrast, deletion of the first N-terminal 12 residues abolished the DNA binding capability of InsA. These results indicate that the DNA binding domain of InsA is located at its N terminus.

This article has been cited by other articles:

• Egelseer, E. M., Idris, R., Jarosch, M., Danhorn, T., Sleytr, U. B., Sara, M. (2000). ISBst12, a novel type of insertion-sequence element causing loss of S-layer-gene expression in Bacillus stearothermophilus ATCC 12980. Microbiology 146: 2175-2183 [Abstract] [Full Text]  
• Skaugen, M., Nes, I. F. (2000). Transposition in Lactobacillus sakei: inactivation of a second lactocin S operon by the insertion of IS1520, a new member of the IS3 family of insertion sequences. Microbiology 146: 1163-1169 [Abstract] [Full Text]  
• Hu, S.-T., Wang, H.-C., Lei, G.-S., Wang, S.-H. (1998). Negative Regulation of IS2 Transposition by the Cyclic AMP (cAMP)-cAMP Receptor Protein Complex. J. Bacteriol. 180: 2682-2688 [Abstract] [Full Text]