Interactions that drive Sec-dependent bacterial protein transport.

Interactions that drive Sec-dependent bacterial protein transport. Research Abstract Details 

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Interactions that drive Sec-dependent bacterial protein transport. Abstract Text:

Sharyn L Rusch,Debra A Kendall,

Understanding the transport of hydrophilic proteins across biological membranes continues to be an important undertaking. The general secretory (Sec) pathway in Escherichia coli transports the majority of E. coli proteins from their point of synthesis in the cytoplasm to their sites of final localization, associating sequentially with a number of protein components of the transport machinery. The targeting signals for these substrates must be discriminated from those of proteins transported via other pathways. While targeting signals for each route have common overall characteristics, individual signal peptides vary greatly in their amino acid sequences. How do these diverse signals interact specifically with the proteins that comprise the appropriate transport machinery and, at the same time, avoid targeting to an alternate route? The recent publication of the crystal structures of components of the Sec transport machinery now allows a more thorough consideration of the interactions of signal sequences with these components.

Interactions that drive Sec-dependent bacterial protein transport. Publishing Authors By Initials

SL Rusch,DA Kendall,

For similar biological phenomena, cell phenomena, and immunity: cell physiology: cell communication: signal transduction research abstracts see: biological phenomena, cell phenomena, and immunity: cell physiology: cell communication: signal transduction research

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Interactions that drive Sec-dependent bacterial protein transport. Journal Published:

PUBLICATION TYPE: Review

Journal: Biochemistry

VOLUME: 46

Page Numbers: 9665-73

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 3

MONTH: 08

YEAR: 2007

Interactions that drive Sec-dependent bacterial protein transport. Information

Number of References: 113

LANGUAGE: eng

NlmUniqueID: 370623

Interactions that drive Sec-dependent bacterial protein transport. Keywords Mesh Terms:

KEYWORDS: Signal Transduction

MESH TERMS: genetics

Chemical & Substance for Abstract: Interactions that drive Sec-dependent bacterial protein transport. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Interactions that drive Sec-dependent bacterial protein transport.

AFFILIATION: Department of Molecular and Cell Biology, The University of Connecticut, Storrs, Connecticut 06269-3125, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM37639

ACRONYM: GM

MEDLINETA: Biochemistry

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