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Biogenesis, transport and remodeling of lysophospholipids in Gram-negative bacteria.
Zheng, Lei; Lin, Yibin; Lu, Shuo; Zhang, Jiazhe; Bogdanov, Mikhail.
Afiliação
  • Zheng L; Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA. Electronic address: lei.zheng@uth.tmc.edu.
  • Lin Y; Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
  • Lu S; Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
  • Zhang J; Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
  • Bogdanov M; Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
Biochim Biophys Acta Mol Cell Biol Lipids ; 1862(11): 1404-1413, 2017 Nov.
Article em En | MEDLINE | ID: mdl-27956138
ABSTRACT
Lysophospholipids (LPLs) are metabolic intermediates in bacterial phospholipid turnover. Distinct from their diacyl counterparts, these inverted cone-shaped molecules share physical characteristics of detergents, enabling modification of local membrane properties such as curvature. The functions of LPLs as cellular growth factors or potent lipid mediators have been extensively demonstrated in eukaryotic cells but are still undefined in bacteria. In the envelope of Gram-negative bacteria, LPLs are derived from multiple endogenous and exogenous sources. Although several flippases that move non-glycerophospholipids across the bacterial inner membrane were characterized, lysophospholipid transporter LplT appears to be the first example of a bacterial protein capable of facilitating rapid retrograde translocation of lyso forms of glycerophospholipids across the cytoplasmic membrane in Gram-negative bacteria. LplT transports lyso forms of the three bacterial membrane phospholipids with comparable efficiency, but excludes other lysolipid species. Once a LPL is flipped by LplT to the cytoplasmic side of the inner membrane, its diacyl form is effectively regenerated by the action of a peripheral enzyme, acyl-ACP synthetase/LPL acyltransferase (Aas). LplT-Aas also mediates a novel cardiolipin remodeling by converting its two lyso derivatives, diacyl or deacylated cardiolipin, to a triacyl form. This coupled remodeling system provides a unique bacterial membrane phospholipid repair mechanism. Strict selectivity of LplT for lyso lipids allows this system to fulfill efficient lipid repair in an environment containing mostly diacyl phospholipids. A rocker-switch model engaged by a pair of symmetric ion-locks may facilitate alternating substrate access to drive LPL flipping into bacterial cells. This article is part of a Special Issue entitled Bacterial Lipids edited by Russell E. Bishop.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Lisofosfolipídeos / Parede Celular / Proteínas de Transferência de Fosfolipídeos / Lipogênese / Bactérias Gram-Negativas Tipo de estudo: Prognostic_studies Idioma: En Revista: Biochim Biophys Acta Mol Cell Biol Lipids Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Lisofosfolipídeos / Parede Celular / Proteínas de Transferência de Fosfolipídeos / Lipogênese / Bactérias Gram-Negativas Tipo de estudo: Prognostic_studies Idioma: En Revista: Biochim Biophys Acta Mol Cell Biol Lipids Ano de publicação: 2017 Tipo de documento: Article