title: Molecular dissection of the Selenomonas ruminantium cell envelope and lysine decarboxylase involved in the biosynthesis of a polyamine covalently linked to the cell wall peptidoglycan layer.
abstract: The wild type of Selenomonas ruminantium subsp. lactilytica, which is a strictly anaerobic, Gram-negative bacterium isolated from sheep rumen, requires one of the normal saturated volatile fatty acids with 3 to 10 carbon atoms for its growth in a glucose medium; however, no such obligate requirement of fatty acid is observed when the cells are grown in a lactate medium. This bacterium is characterized by a unique structure of the cell envelope and a novel lysine decarboxylase and its regulatory protein. In the first part of this article, we will refer to the chemical structure of phospholipid and lipopolysaccharide in the cell membranes of this bacterium compared with that from the general Gram-negative bacteria for understanding their biological functions. S. ruminantium has neither free nor bound forms of Braun lipoprotein which plays an important role of the maintenance of the structural integrity of the cell surface in general Gram-negative bacteria. However, S. ruminantium has cadaverine, which links covalently to the peptidoglycan as a pivotal constituent for the cell division. In the second part of this article, we will refer to the chemical structure of the cadaverine-containing peptidoglycan, its biosynthesis, and the biological function. In the third part of this article, we will depict the molecular cloning of the genes encoding S. ruminanitum lysine decarboxylase (LDC) and its regulatory protein of 22-kDa (22-kDa protein; P22) which has similar characteristics to that of antizyme of ornithine decarboxylase in eukaryotic cells, and the molecular dissection of these proteins for understanding the regulation of cadaverine biosynthesis. Finally, we will illustrate a proposed structure of the cell envelope, a processes of biosynthesis of the cadaverine-containing peptidoglycan layer, and the LDC degradation mechanism in S. ruminantium, on the basis of the analyses of the cell envelope components, the results from the in vitro experiments on the biosynthesis of the peptidoglycan layer, and the current status of the knowledge on LDC and P22 in this organism.
authors.affiliation: Laboratory of Applied Microbiology, Department of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
authors.forename: Yumiko
authors.initials: Y
authors.lastname: Takatsuka
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Kamio
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002262:Carboxy-Lyases / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism; D003001:Cloning, Molecular; D003959:Diamines / Q000737:chemistry; D019143:Evolution, Molecular; D008070:Lipopolysaccharides / Q000737:chemistry / Q000378:metabolism; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism*; D011073:Polyamines / Q000737:chemistry / Q000378:metabolism*; D020357:Selenomonas / Q000166:cytology* / Q000378:metabolism*; D014678:Veillonella / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D003959:Diamines; D008070:Lipopolysaccharides; D010457:Peptidoglycan; D011073:Polyamines; D002262:Carboxy-Lyases; C021520:lysine decarboxylase