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Studying bacterial chemosensory array with CryoEM.
Qin, Zhuan; Zhang, Peijun.
Afiliação
  • Qin Z; Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, U.K.
  • Zhang P; Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, U.K.
Biochem Soc Trans ; 49(5): 2081-2089, 2021 11 01.
Article em En | MEDLINE | ID: mdl-34495335
ABSTRACT
Bacteria direct their movement in respond to gradients of nutrients and other stimuli in the environment through the chemosensory system. The behavior is mediated by chemosensory arrays that are made up of thousands of proteins to form an organized array near the cell pole. In this review, we briefly introduce the architecture and function of the chemosensory array and its core signaling unit. We describe the in vivo and in vitro systems that have been used for structural studies of chemosensory array by cryoEM, including reconstituted lipid nanodiscs, 2D lipid monolayer arrays, lysed bacterial ghosts, bacterial minicells and native bacteria cells. Lastly, we review recent advances in structural analysis of chemosensory arrays using state-of-the-art cryoEM and cryoET methodologies, focusing on the latest developments and insights with a perspective on current challenges and future directions.
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Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Transdução de Sinais / Quimiotaxia / Microscopia Crioeletrônica / Proteínas de Escherichia coli / Escherichia coli / Histidina Quinase / Proteínas Quimiotáticas Aceptoras de Metil Idioma: En Revista: Biochem Soc Trans Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Reino Unido

Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Transdução de Sinais / Quimiotaxia / Microscopia Crioeletrônica / Proteínas de Escherichia coli / Escherichia coli / Histidina Quinase / Proteínas Quimiotáticas Aceptoras de Metil Idioma: En Revista: Biochem Soc Trans Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Reino Unido