Characterization of the mycoplasma membrane proteins II. Solubilization and enzymic activities of Acholeplasma laidlawii membrane proteins

Ne'eman, Zvi; Kahane, Itzhak; Razin, Shmuel

doi:10.1016/0005-2736(71)90093-9

Cited by 78 publications

(29 citation statements)

References 23 publications

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“…Such nonspecific enzymes that hydrolyze dUTP and dCTP include nucleoside triphosphatase (1, 9), adenosine triphosphatase (8), and alkaline phosphatase (3). Both adenosine triphosphatase (6,16) and an alkaline phosphatase-like activity (12) have been reported in extracts of A . laidlawii.…”

Section: Methodsmentioning

confidence: 99%

Pyrimidine Deoxyribonucleotide Metabolism in Members of the Class Mollicutes

Williams

Pollack²

1985

International Journal of Systematic Bacteriology

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Cell extracts from six Acholeplasma species, six Mycoplasma species, and Spiroplasma Jlwicola 23-6T (T = type strain) were examined for enzyme activities of pyrimidine deoxyribonucleotide metabolism. A11 of these organisms had thymidine kinase and thymidine phosphorylase activities, and all lacked deoxycytidine triphosphatase activity. The 13 members of the Mollicutes were separated into three groups by the presence or absence of the following four enzyme activities: (i) the adenosine triphosphate-insensitive deoxyuridine triphosphate-specific hydrolyzing deoxyuridine triphosphatase, (ii) a deoxyuridine monophosphate phosphatase, (iii) deoxycytidine deaminase, and (iv) deoxycytidine monophosphate deaminase. Five of the six Acholeplasma species (all Acholeplasma species except Acholeplasma florum LIT) had all four enzymatic activities. The six Mycoplasma species only had the deoxycytidine and deoxycytidine monophosphate deaminase activities. The only two plant isolates studied, A . Jlorum LIT and S . Jloricola 23-6T, lacked all four enzymatic activities.The class Mollicutes contains two orders. The order Mycoplasmatales is composed of two families, the Mycoplasmataceae, which has two genera (Mycoplasma and Ureaplasma), and the Spiroplasmataceae, which has o n e genus ( S p i r o p l a s m a ) (4). The second order, A c h o l e p l a s m a t a l e s , c o n t a i n s o n e f a m i l y , t h e Achdeplasmataceae, with one genus, Acholeplasma (5). A number of biochemical, nutritional, and morphological characteristics have been used to distinguish these genera and families. They include sterol requirement for growth, genome sizes, ability to hydrolyze urea, localization of reduced nicotinamide adenine dinucleotide oxidase, and presence of helical forms during growth (4, 5). However, no one has distinguished genera or families of the Mollicutes by the presence or absence of enzymes involved in pyrimidine deoxyribonucleotide metabolism.Recently, we characterized the adenosine triphosphate (ATP)-insensitive highly specific deoxyuridine triphosphate ( d U T P ) -h y d r 01 y zi ng d e o x y uri d i n e t r i p h o s p h a t e nucleotidohydrolase (dUTPase; EC 3.6.1.23) from Acholeplasma laidlawii B-PG9 (17). In the present study, we examined five other Acholeplasma species, six Mycoplasma species, and one Spiroplasma species for dUTPase and o t h e r e n z y m e a c t i v i t i e s involved in pyrimidine deoxyribonucleotide metabolism. Our data suggest that it may be possible, with one exception, to distinguish these genera based upon the presence or absence of the ATP-insensitive dUTP-specific dUTPase (17), deoxyuridine monophosphate (dUMP) phosphatase, deoxycytidine (dC) deaminase, and deoxycytidine monophosphate (dCMP) deaminase activities in cell extracts. (56.6 Ci/mmol) were purchased from Amersham Corp., Arlington Heights, Ill. Polyethyleneimine-cellulose thinlayer chromatography plates were purchased from Analtech, Newark, Del. MATERIALS AND METHODSOrganisms. Acholeplasma florum LIT (T = type strain) and Spiroplasm...

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Section: Methodsmentioning

confidence: 99%

Pyrimidine Deoxyribonucleotide Metabolism in Members of the Class Mollicutes

Williams

Pollack²

1985

International Journal of Systematic Bacteriology

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“…It is not known what determines the antigenicity of individual proteins, whether it be a specific hapten or configuration, or simply availability for interaction in the immune system. Antigenic differences among mycoplasma proteins have been observed between different fractions of solubilized Acholeplasma laidlawii proteins separated by gel filtration (Ne'eman et al, 1972) and by crossed immunoelectrophoresis of solubilized mycoplasma proteins (Thirkill & Kenny, 1974;Johansson & Hjerten, 1974). Protein A, a major membrane-associated protein of LC strains of subsp.…”

Section: Discussionmentioning

confidence: 99%

Immunoprecipitation of Triton X-100-solubilized Mycoplasma mycoides Proteins

Archer

1979

Journal of General Microbiology

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111Mycoplasma mycoides subsp. mycoides (PG1 and strain Y) proteins were solubilized in Triton X-100, and the antigenic proteins were precipitated from this complex mixture by addition of antiserum and then separated by two-dimensional gel electrophoresis. Of the 300 proteins solubilized, about 10 were precipitated. Proteins of PG1, a slow-growing, small colony (SC) strain, were precipitated by antiserum to PG1 and by antiserum to strain Y, a fast-growing, large colony (LC) strain. Similarly, strain Y proteins were precipitated by antiserum to PG1 and by antiserum to strain Y. The few proteins precipitated in this way gave similar patterns after two-dimensional gel electrophoresis indicating that many of the dominant protein antigens of PG1 and strain Y are shared. Antiserum to Mycoplasma mycoides subsp. Capri (PG3) also precipitated some proteins of strain Y. Antiserum to Mycoplasma gallisepticum gave no reaction with any M . mycoides antigens. It was concluded that, in addition to the polysaccharide antigens, there are proteins in M. mycoides that are antigenic and that some of these are found in both the SC and LC strains of subsp. mycoides and also in subsp. Capri.

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“…The idea is intriguing since P. F. Smith has shown that the presence of some lipids of these genera, almost entirely in the membrane, may be taxonomically distinguishing (29,30). However, Ne'eman et al (16) have shown that NADH oxidase activity isolated from A . laidlawii membranes with detergent does not require the presence of membrane lipids.…”

Section: Discussionmentioning

confidence: 99%

Localization of Reduced Nicotinamide Adenine Dinucleotide Oxidase Activity in Acholeplasma and Mycoplasma Species

Pollack

1975

International Journal of Systematic Bacteriology

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Characterization of the mycoplasma membrane proteins II. Solubilization and enzymic activities of Acholeplasma laidlawii membrane proteins

Cited by 78 publications

References 23 publications

Pyrimidine Deoxyribonucleotide Metabolism in Members of the Class Mollicutes

Pyrimidine Deoxyribonucleotide Metabolism in Members of the Class Mollicutes

Immunoprecipitation of Triton X-100-solubilized Mycoplasma mycoides Proteins

Localization of Reduced Nicotinamide Adenine Dinucleotide Oxidase Activity in Acholeplasma and Mycoplasma Species

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