Identification and characterization of xcpR encoding a subunit of the general secretory pathway necessary for dodecane degradation in Acinetobacter calcoaceticus ADP1

Parche, Stephan; Geißdörfer, Walter; Hillen, Wolfgang

doi:10.1128/jb.179.14.4631-4634.1997

Cited by 27 publications

(36 citation statements)

References 35 publications

(15 reference statements)

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“…The exoenzymes previously found lacking from pilD or other type II secretion mutants include the following: the esterase and lipase of Acinetobacter calcoaceticus; the acyltransferase, aerolysin, and protease of A. hydrophila; the lipases of Burkholderia sp. ; the pectate lyase and cellulase of Erwinia chrysanthemi; the pullulanase of Klebsiella oxytoca; the alkaline phosphatase, lipase, elastase, exotoxin A, LasA protease, and PLC of P. aeruginosa; the cholera toxin, protease, and endochitinase of V. cholerae; and the amylase, cellulase, endoglucanase, and protease of Xanthomonas campestris (14,20,24,33,36,44,55,56,58,63,70). Thus, there is precedent for a linkage between pilD and an esterase-lipase and protease.…”

Section: Discussionmentioning

confidence: 99%

Secreted Enzymatic Activities of Wild-Type and pilD -Deficient Legionella pneumophila

et al. 2000

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Legionella pneumophila, the agent of Legionnaires' disease, is an intracellular pathogen of protozoa and macrophages. Previously, we had determined that the Legionella pilD gene is involved in type IV pilus biogenesis, type II protein secretion, intracellular infection, and virulence. Since the loss of pili and a protease do not account for the infection defect exhibited by a pilD-deficient strain, we sought to define other secreted proteins absent in the mutant. Based upon the release of p-nitrophenol (pNP) from p-nitrophenyl phosphate, acid phosphatase activity was detected in wild-type but not in pilD mutant supernatants. Mutant supernatants also did not release either pNP from p-nitrophenyl caprylate and palmitate or free fatty acid from 1-monopalmitoylglycerol, suggesting that they lack a lipase-like activity. However, since wild-type samples failed to release free fatty acids from 1,2-dipalmitoylglycerol or to cleave a triglyceride derivative, this secreted activity should be viewed as an esterase-monoacylglycerol lipase. The mutant supernatants were defective for both release of free fatty acids from phosphatidylcholine and degradation of RNA, indicating that PilD-negative bacteria lack a secreted phospholipase A (PLA) and nuclease. Finally, wild-type but not mutant supernatants liberated pNP from p-nitrophenylphosphorylcholine (pNPPC). Characterization of a new set of mutants defective for pNPPC-hydrolysis indicated that this wild-type activity is due to a novel enzyme, as opposed to a PLC or another known enzyme. Some, but not all, of these mutants were greatly impaired for intracellular infection, suggesting that a second regulator or processor of the pNPPC hydrolase is critical for L. pneumophila virulence.

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Section: Discussionmentioning

confidence: 99%

Secreted Enzymatic Activities of Wild-Type and pilD -Deficient Legionella pneumophila

et al. 2000

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“…The xcpR gene encodes a type IV pilus-related system that may not only be required for the secretion of proteins but may represent a more universal transport system for a variety of macromolecules. It may also facilitate the alleviation of membrane stress incurred by bacterial cells during alkane degradation (Parche et al, 1997). All genes except lipB gene demonstrated a similar pattern.…”

Section: The Target Gene Expressions and Comparison Between Lt 1 And mentioning

confidence: 61%

“…ADP1 and DSM 17874 strains (Parche et al, 1997;Throne-Holst et al, 2007). The expression of xcpR in conjunction with rubA and rubB in A. calcoaceticus is known to be constitutive (Ratajczak et al, 1998).…”

Section: The Target Gene Expressions and Comparison Between Lt 1 And mentioning

confidence: 99%

“…The alkM gene expression is regulated by the alkane hydroxylase regulator (alkR) (Ratajczak et al, 1998). The participation of xcpR gene in alkane degradation was proposed in A. calcoaceticus ADP1 after the insertional inactivation of xcpR impeded the secretion of lipase and esterase that lead to the lack of growth on dodecane and slower growth on hexadecane (Parche et al, 1997). In A. calcoaceticus ADP1, the estB gene encodes a functional esterase and is localized in an operon with genes rubA, rubB and oxyR (Geißdörfer et al 1999).…”

Section: Introductionmentioning

confidence: 99%

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Quantitative PCR analysis of diesel degrading genes of Acinetobacter calcoaceticus isolates

Lin

Sharma²

2013

Afr. J. Microbiol. Res.

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Acinetobacter strains LT 1 and V 2 were grown in Bushnell-Haas medium with 1% diesel and their expression levels of eight diesel-degrading genes were evaluated by quantitative polymerase chain reaction (PCR). LT 1 and V 2 isolates achieved 86.2 and 89.7% degradation respectively, after 60 days with no significant differences in expression, in comparison with 16S rRNA, rubB and lipB. LT 1 showed higher expression levels of rubA, alkM, alkR and xcpR genes during the initial stages of incubation corresponding to higher level of degradation rate. Amplification of alkM, alkR and xcpR genes of V 2 indicated more than one enzyme system involved in the process. Low lipB and lipA expression in LT 1 and no lipA expression in V 2 suggested the absence of lipases in degradation; however, estB gene was predominantly expressed in V 2 . Thus, isolates LT 1 and V 2 possessed comparable efficiency in degrading diesel; however, more complex systems have been employed by V 2 i n degradation process.

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“…These three strains were recently grouped within one newly delineated species, A. baylyi (Young et al, 2005). Strain ADP1 was also referred to as A. calcoaceticus ADP1 (Geissdorfer et al, 1995Parche et al, 1997;Williams and Shaw, 1997; Kalscheuer and Steinbuchel, 2003; Krehenbrinkand Steinbuchel, 2004;Elbahloul et al, 2005), or more often as Acinetobacter sp. ADP1 (Barbe et al, 2004).…”

Section: The Use Of Species Names In the Literaturementioning

confidence: 99%

Safety Assessment of Transgenic Organisms, Volume 4

2010

Harmonisation of Regulatory Oversight in Biotechnology

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show abstract

Identification and characterization of xcpR encoding a subunit of the general secretory pathway necessary for dodecane degradation in Acinetobacter calcoaceticus ADP1

Cited by 27 publications

References 35 publications

Secreted Enzymatic Activities of Wild-Type and pilD -Deficient Legionella pneumophila

Secreted Enzymatic Activities of Wild-Type and pilD -Deficient Legionella pneumophila

Quantitative PCR analysis of diesel degrading genes of Acinetobacter calcoaceticus isolates

Safety Assessment of Transgenic Organisms, Volume 4

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