| Literature DB >> 10234833 |
G Layh-Schmitt1, M Harkenthal.
Abstract
After Triton X-100 treatment of Mycoplasma pneumoniae cells, a portion of the adhesin P1 (transmembrane protein) proved to remain tightly associated with the Triton insoluble material (Triton shell) as shown previously by several authors. However, the spontaneous loss of two cytadherence-associated membrane proteins of 90 and 40 kDa (gene product of the open reading frame 6 of the P1 operon) in a hemadsorption-negative mutant, designated M5, resulted in a 100% release of the P1 protein into the Triton phase and in the lack of the characteristic tip-like attachment organelle of M. pneumoniae indicating an essential role of the open reading frame 6 gene product in tip structure formation.Entities:
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Year: 1999 PMID: 10234833 DOI: 10.1111/j.1574-6968.1999.tb13561.x
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742