This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal 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 Valdes-Stauber, N. Articles by Scherer, S. Search for Related Content PubMed PubMed Citation Articles by Valdes-Stauber, N. Articles by Scherer, S. Agricola Articles by Valdes-Stauber, N. Articles by Scherer, S.

 Previous Article  |  Next Article 

Appl. Environ. Microbiol., Apr 1996, 1283-1286, Vol 62, No. 4
Copyright © 1996, American Society for Microbiology

Nucleotide sequence and taxonomical distribution of the bacteriocin gene lin cloned from Brevibacterium linens M18

N Valdes-Stauber and S Scherer
Institut fur Mikrobiologie, Technische Universitat Munchen, Freising, Germany.

Linocin M18 is an antilisterial bacteriocin produced by the red smear cheese bacterium Brevibacterium linens M18. Oligonucleotide probes based on the N-terminal amino acid sequence were used to locate its single copy gene, lin, on the chromosomal DNA. The amino acid composition, N-terminal sequence, and molecular mass derived from the nucleotide sequence of an open reading frame of 798 nucleotides coding for 266 amino acids found on a 3-kb BamHI restriction fragment correspond closely to those obtained from the purified protein (N. Valdes-Stauber and S. Scherer, Appl. Environ. Microbiol. 60:3809-3814, 1994). No sequence homology to any protein or nucleotide sequences deposited in databases was found. Comparison of the nucleotide sequence and the N-terminal amino acid sequence derived from the protein suggests that B. linens M18 produces an N-formyl-methionyl-CAC tRNA. A wide taxonomical distribution of the gene within coryneform bacteria has been demonstrated by PCR amplification. The structural gene from linocin M18 is present at least in three Brevibacterium species, five Arthrobacter species, and five Corynebacterium species.

This article has been cited by other articles:

• Pysz, M. A., Conners, S. B., Montero, C. I., Shockley, K. R., Johnson, M. R., Ward, D. E., Kelly, R. M. (2004). Transcriptional Analysis of Biofilm Formation Processes in the Anaerobic, Hyperthermophilic Bacterium Thermotoga maritima. Appl. Environ. Microbiol. 70: 6098-6112 [Abstract] [Full Text]  
• Nilsen, T., Nes, I. F., Holo, H. (2003). Enterolysin A, a Cell Wall-Degrading Bacteriocin from Enterococcus faecalis LMG 2333. Appl. Environ. Microbiol. 69: 2975-2984 [Abstract] [Full Text]  
• Carnio, M. C., Höltzel, A., Rudolf, M., Henle, T., Jung, G., Scherer, S. (2000). The Macrocyclic Peptide Antibiotic Micrococcin P1 Is Secreted by the Food-Borne Bacterium Staphylococcus equorum WS 2733 and Inhibits Listeria monocytogenes on Soft Cheese. Appl. Environ. Microbiol. 66: 2378-2384 [Abstract] [Full Text]  
• Rosenkrands, I., Rasmussen, P. B., Carnio, M., Jacobsen, S., Theisen, M., Andersen, P. (1998). Identification and Characterization of a 29-Kilodalton Protein from Mycobacterium tuberculosis Culture Filtrate Recognized by Mouse Memory Effector Cells. Infect. Immun. 66: 2728-2735 [Abstract] [Full Text]