RTX proteins: a highly diverse family secreted by a common mechanism

Linhartová, Irena and Bumba, Ladislav and Mašín, Jiří and Basler, Marek and Osička, Radim and Kamanová, Jana and Procházková, Kateřina and Adkins, Irena and Hejnová-Holubová, Jana and Sadílková, Lenka and Morová, Jana and Sebo, Peter. (2010) RTX proteins: a highly diverse family secreted by a common mechanism. FEMS Microbiology Reviews, 34 (6). pp. 1076-1112.

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Repeats-in-toxin (RTX) exoproteins of Gram-negative bacteria form a steadily growing family of proteins with diverse biological functions. Their common feature is the unique mode of export across the bacterial envelope via the type I secretion system and the characteristic, typically nonapeptide, glycine- and aspartate-rich repeats binding Ca(2+) ions. In this review, we summarize the current state of knowledge on the organization of rtx loci and on the biological and biochemical activities of therein encoded proteins. Applying several types of bioinformatic screens on the steadily growing set of sequenced bacterial genomes, over 1000 RTX family members were detected, with the biological functions of most of them remaining to be characterized. Activities of the so far characterized RTX family members are then discussed and classified according to functional categories, ranging from the historically first characterized pore-forming RTX leukotoxins, through the large multifunctional enzymatic toxins, bacteriocins, nodulation proteins, surface layer proteins, up to secreted hydrolytic enzymes exhibiting metalloprotease or lipase activities of industrial interest.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Infection Biology > Infection Biology (Basler)
UniBasel Contributors:Basler, Marek
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:25 Apr 2018 07:52
Deposited On:25 Apr 2018 07:52

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