A Complex Lipoate Utilization Pathway in Listeria monocytogenes

被引：28

作者：

Christensen, Quin H. ^{[3
]}

Hagar, Jon A. ^{[4
]}

O'Riordan, Mary X. D. ^{[4
]}

Cronan, John E. ^{[1
,2
,3
]}

机构：

[1] Univ Illinois, Dept Microbiol, Chem & Life Sci Lab, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

[3] Univ Illinois, Chem Biol Interface Training Program, Urbana, IL 61801 USA

[4] Univ Michigan, Sch Med, Dept Microbiol & Immunol, Ann Arbor, MI 48109 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2011年 / 286卷 / 36期

基金：

美国国家卫生研究院;

关键词：

LIPOIC ACID SYNTHESIS; INTRACELLULAR GROWTH; ESCHERICHIA-COLI; FATTY-ACIDS; CLONING; LPLA; METABOLISM; ATTACHMENT; EXPRESSION; FAMILY;

D O I：

10.1074/jbc.M111.273607

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Although a complete pathway of lipoic acid metabolism has been established in Escherichia coli, lipoic acid metabolism in other bacteria is more complex and incompletely understood. Listeria monocytogenes has been shown to utilize two lipoate-protein ligases for lipoic acid scavenging, whereas only one of the ligases can function in utilization of host-derived lipoic acid-modified peptides. We report that lipoic acid scavenging requires not only ligation of lipoic acid but also a lipoyl relay pathway in which an amidotransferase transfers lipoyl groups to the enzyme complexes that require the cofactor for activity. In addition, we provide evidence for a new lipoamidase activity that could allow utilization of lipoyl peptides by lipoate-protein ligase. These data support a model of an expanded, three-enzyme pathway for lipoic acid scavenging that seems widespread in the Firmicutes phylum of bacteria.

引用

页码：31447 / 31456

页数：10

共 29 条

[1] Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli [J].

Anjem, Adil ;

Varghese, Shery ;

Imlay, James A. .

MOLECULAR MICROBIOLOGY, 2009, 72 (04) :844-858

[2]

[Anonymous], 2012, Molecular Cloning: A Laboratory Manual

[3] A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis [J].

Christensen, Quin H. ;

Martin, Natalia ;

Mansilla, Maria C. ;

de Mendoza, Diego ;

Cronan, John E. .

MOLECULAR MICROBIOLOGY, 2011, 80 (02) :350-363

[4] Lipoic Acid Synthesis: A New Family of Octanoyltransferases Generally Annotated as Lipoate Protein Ligases [J].

Christensen, Quin H. ;

Cronan, John E. .

BIOCHEMISTRY, 2010, 49 (46) :10024-10036

[5] The Thermoplasma acidophilum LplA-LplB Complex Defines a New Class of Bipartite Lipoate-protein Ligases [J].

Christensen, Quin H. ;

Cronan, John E. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (32) :21317-21326

[6] Function, attachment and synthesis of lipoic acid in Escherichia coli [J].

Cronan, JE ;

Zhao, X ;

Jiang, YF .

ADVANCES IN MICROBIAL PHYSIOLOGY, VOL 50, 2005, 50 :103-146

[7] Investigation of the Mechanisms by Which Listeria monocytogenes Grows in Porcine Gallbladder Bile [J].

Dowd, Georgina C. ;

Joyce, Susan A. ;

Hill, Colin ;

Gahan, Cormac G. M. .

INFECTION AND IMMUNITY, 2011, 79 (01) :369-379

[8]

Eschenfeldt William H., 2009, V498, P105, DOI 10.1007/978-1-59745-196-3_7

[9] The Pfam protein families database [J].

Finn, Robert D. ;

Mistry, Jaina ;

Tate, John ;

Coggill, Penny ;

Heger, Andreas ;

Pollington, Joanne E. ;

Gavin, O. Luke ;

Gunasekaran, Prasad ;

Ceric, Goran ;

Forslund, Kristoffer ;

Holm, Liisa ;

Sonnhammer, Erik L. L. ;

Eddy, Sean R. ;

Bateman, Alex .

NUCLEIC ACIDS RESEARCH, 2010, 38 :D211-D222

[10] Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP [J].

Fujiwara, Kazuko ;

Hosaka, Harumi ;

Matsuda, Makoto ;

Okamura-Ikeda, Kazuko ;

Motokawa, Yutaro ;

Suzuki, Mamoru ;

Nakagawa, Atsushi ;

Taniguchi, Hisaaki .

JOURNAL OF MOLECULAR BIOLOGY, 2007, 371 (01) :222-234

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