NDLI: Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: interesting implications and applications

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Molecular BioSystems Vol - 6 Issue - 5

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Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: interesting implications and applications

Content Provider	Royal Society of Chemistry (RSC)
Author	Shruthi, Hamsanathan Sankaran, Krishnan Anand, Prakash Murugan, Vadivel
Copyright Year	2010
Abstract	Bacterial lipoproteins, an important class of membrane proteins, are generally thought to be translocated in an unfolded state by the well-studied Sec machinery, whereas the role of TAT, meant for folded proteins, is hardly investigated. Using appropriately engineered fast-folding Enhanced Green Fluorescence Protein (EGFP), as a model, here we show that TAT is essential for not only translocating fast-folding lipoprotein but also its lipid modification. EGFP was lipid-modified and targeted to the outer membrane's outer surface with a prototypical TAT signal sequence containing lipobox but not with the lipoprotein or TAT signal sequence. Justifiably signal sequences of many substrate-binding and co-factor-containing lipoproteins contained both TAT-box and lipobox (Shruthi et al., submitted). Cytoplasmic accumulation of unmodified precursors of engineered EGFP in a tatC mutant implicated this TAT-box-recognizing component in lipid-modification. Similar observations reported earlier with Sec components and murein lipoprotein led us to propose that the translocation-competent and translocase-associated (Sec or TAT) precursor form is prerequisite to initiation of lipid-modification in vivo. The above missing links between translocation and lipid modification machineries in vivo is important to our understanding of bacterial lipoprotein biosynthesis and its utility as a protein engineering tool for potent applications in synthetic biology and nanobiotechnology like display, arrays on bacterial surfaces, vaccines and biosensors.
Starting Page	999
Ending Page	1007
Page Count	9
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	6
Issue Number	6
Journal	Molecular BioSystems
DOI	10.1039/b916510j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Sec Peptidoglycan Protein engineering TAT Green fluorescent protein Lipoprotein Mutation EGFP Molecular biology Lipid Nanobiotechnology
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein

Genetic evidence for a tatc dimer at the core of the escherichia coli twin arginine (tat) protein translocase.

Assembling the Tat protein translocase.

Genetic Analysis of the Twin Arginine Translocator Secretion Pathway in Bacteria

Constitutive expression of escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth (2000).

Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein

Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).

Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase.

Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase

Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: interesting implications and applications

Similar Documents

Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein

Genetic evidence for a tatc dimer at the core of the escherichia coli twin arginine (tat) protein translocase.

Assembling the Tat protein translocase.

Genetic Analysis of the Twin Arginine Translocator Secretion Pathway in Bacteria

Constitutive expression of escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth (2000).

Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein

Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).

Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase.

Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase

Twin arginine translocase pathway and fast-folding lipoprotein biosynthesis in E. coli: interesting implications and applications