Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSelvan, A Tamil-
dc.contributor.authorSankaran, K-
dc.identifier.issn0975-0967 (Online); 0972-5849 (Print)-
dc.description.abstractLipid modification is an emerging protein-engineering tool for providing hydrophobic anchor to hydrophilic proteins for immobilizing them onto a variety of man-made and biological surfaces. In this respect, N-acyl S-diacylglyceryl modification of N-terminal cysteine, called bacterial lipid modification has many advantages including the fact that it can be achieved through popular prokaryotic expression of proteins. The modification proceeds in a three-step cascade reaction in which three inner membrane enzymes, Phosphatidylglycerol:Prolipoprotein diacylglyceryl transferase, signal peptidase II and apolipoprotein N-acyl transferase, participate. Bacterial expression has limitations including the necessity of expensive downstream processing. However, in vitro modification has not been possible so far because the enzymology of this pathway is not well studied due to difficulty in assaying these enzymes. As a first step to overcome this problem we have designed the peptide substrate, MKATKSAVGSTLAGCSSHHHHHH, for in vitro lipid modification specifically the first enzyme, Phosphatidylglycerol:Prolipoprotein diacylglyceryl transferase, which catalyzes the committed step. The design was based on bioinformatics analysis of more than 1000 bacterial lipoprotein precursors. This synthetic peptide substrate was soluble and contained other built-in features useful in easier handling and purification. The designed substrate exhibited expected properties and in vitro diacylglyceryl modification was confirmed by Tricine SDS PAGE based mobility shift assay.en_US
dc.relation.ispartofseriesInt. Cl.8 C12N1/38en_US
dc.sourceIJBT Vol.5(3) [July 2006]en_US
dc.subjectbacterial lipid modificationen_US
dc.subjectsignal sequenceen_US
dc.subjectpeptide substrateen_US
dc.titleBacterial lipid modification in vitro: Synthetic peptide substrate for phosphatidylglycerol—Prolipoprotein diacylglyceryl transferaseen_US
Appears in Collections:IJBT Vol.05(3) [July 2006]

Files in This Item:
File Description SizeFormat 
IJBT 5(3) 327-331.pdf276.65 kBAdobe PDFView/Open

Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.