The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex.

The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. Research Abstract Details 

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The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. Abstract Text:

Fabien ,Kenneth Cline,

Tat (twin arginine translocation) systems transport folded proteins across the thylakoid membrane of chloroplasts and the plasma membrane of most bacteria. Tat precursors are targeted by hydrophobic cleavable signal peptides with twin arginine (RR) motifs. Bacterial precursors possess an extended consensus, (S/T)RRXFLK, of which the two arginines and the phenylalanine are essential for efficient transport. Thylakoid Tat precursors possess twin arginines but lack the consensus phenylalanine. Here, we have characterized two stages of precursor binding to the thylakoid Tat signal peptide receptor, the 700-kDa cpTatC-Hcf106 complex. The OE17 precursor tOE17 binds to the receptor by RR-dependant electrostatic interactions and partially dissociates during blue native gel electrophoresis. In addition, the signal peptide of thylakoid-bound tOE17 is highly exposed to the membrane surface, as judged by accessibility to factor Xa of cleavage sites engineered into signal peptide flanking regions. By contrast, tOE17 containing a consensus phenylalanine in place of Val(-20) (V - 20F) binds the receptor more strongly and is completely stable during blue native gel electrophoresis. Thylakoid bound V - 20F is also completely protected from factor Xa at the identical sites. This suggests that the signal peptide is buried deeply in the cpTatC-Hcf106 binding site. We further provide evidence that the proton gradient, which is required for translocation, induces a tighter interaction between tOE17 and the cpTat machinery, similar to that exhibited by V - 20F. This implies that translocation involves a very intimate association of the signal peptide with the receptor complex binding site.

The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. Publishing Authors By Initials

F ,K Cline,

For similar cells: cellular structures: intracellular space: cytoplasm: cytoplasmic structures: organelles: plastids: chloroplasts: thylakoids research abstracts see: cells: cellular structures: intracellular space: cytoplasm: cytoplasmic structures: organelles: plastids: chloroplasts: thylakoids research

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The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 5263-72

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 16

MONTH: 12

YEAR: 2006

The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. Keywords Mesh Terms:

KEYWORDS: Thylakoids

MESH TERMS: metabolism

Chemical & Substance for Abstract: The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. Information

Substance Name: Factor XII

Registry Number: 9001-30-3

Grant and Affiliation Information for The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex.

AFFILIATION: Horticultural Sciences Department and Plant Molecular and Cellular Biology Program, University of Florida, Gainesville, Florida 32611, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01 GM48179

ACRONYM: GM

MEDLINETA: J Biol Chem

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