About: Topology Engineering of Proteins in Vivo Using Genetically Encoded, Mechanically Interlocking SpyX Modules for Enhanced Stability

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Topology Engineering of Proteins in Vivo Using Genetically Encoded, Mechanically Interlocking SpyX Modules for Enhanced Stability
Creator	Song, Bo Cao, Yang Liu, Dong Li, Xiaopeng Liu, Ya-Jie Wu, Wen-Hao Wu, Xia-Ling Zhang, Wen-Bin
source	Medline; PMC
abstract	[Image: see text] Recombinant proteins are traditionally limited to linear configuration. Herein, we report in vivo protein topology engineering using highly efficient, mechanically interlocking SpyX modules named AXB and BXA. SpyX modules are protein domains composed of p53dim (X), SpyTag (A), and SpyCatcher (B). The p53dim guides the intertwining of the two nascent protein chains followed by autocatalytic isopeptide bond formation between SpyTag and SpyCatcher to fulfill the interlocking, leading to a variety of backbone topologies. Direct expression of AXB or BXA produces protein catenanes with distinct ring sizes. Recombinant proteins containing SpyX modules are obtained either as mechanically interlocked obligate dimers if the protein of interest is fused to the N- or C-terminus of SpyX modules, or as star proteins if the protein is fused to both N- and C-termini. As examples, cellular syntheses of dimers of (GB1)(2) (where GB1 stands for immunoglobulin-binding domain B1 of streptococcal protein G) and of four-arm elastin-like star proteins were demonstrated. Comparison of the catenation efficiencies in different constructs reveals that BXA is generally much more effective than AXB, which is rationalized by the arrangement of three domains in space. Mechanical interlocking induces considerable stability enhancement. Both AXB and BXA have a melting point ∼20 °C higher than the linear controls and the BXA catenane has a melting point ~2 °C higher than the cyclic control BX’A. Notably, four-arm elastin-like star proteins demonstrate remarkable tolerance against trypsin digestion. The SpyX modules provide a convenient and versatile approach to construct unconventional protein topologies via the “assembly-reaction” synergy, which opens a new horizon in protein science for stability enhancement and function reinforcement via topology engineering.
has issue date	2017-05-10(xsd:dateTime)
bibo:doi	10.1021/acscentsci.7b00104
bibo:pmid	28573210
has license	no-cc
sha1sum (hex)	cb70928ef1e8112feb2a802c88996237f95a524e
schema:url	https://doi.org/10.1021/acscentsci.7b00104
resource representing a document's title	Topology Engineering of Proteins in Vivo Using Genetically Encoded, Mechanically Interlocking SpyX Modules for Enhanced Stability
has PubMed Central identifier	PMC5445526
has PubMed identifier	28573210
schema:publication	ACS Cent Sci
resource representing a document's body	covid:cb70928ef1e8112feb2a802c88996237f95a524e#body_text
is schema:about of	named entity 'ENGINEERING' named entity 'fused' named entity 'mechanically' named entity 'melting point' named entity 'sizes' named entity 'domain' named entity 'Engineering' named entity 'Interlocking' named entity 'PROTEINS' named entity 'C-TERMINUS' named entity 'FOLLOWED BY' named entity 'FORMATION' named entity 'PROVIDE' named entity 'EFFICIENCIES' named entity 'OPENS' named entity 'ENGINEERING' named entity 'HORIZON' named entity 'TOPOLOGY' named entity 'EXPRESSION' named entity 'STAR' named entity 'ARM' named entity 'HAVE' named entity 'COMPOSED OF' named entity 'CONSIDERABLE' named entity 'STANDS' named entity 'REACTION' named entity 'ISOPEPTIDE BOND' named entity 'EITHER' named entity 'SPACE' named entity 'OF INTEREST' named entity 'MECHANICAL' named entity 'HIGHLY' named entity 'APPROACH' named entity 'TOLERANCE' named entity 'DIFFERENT' named entity 'OBLIGATE' covid:arg/cb70928ef1e8112feb2a802c88996237f95a524e named entity 'GENERALLY' named entity 'RING' named entity 'DIRECT' named entity 'LINEAR' named entity 'OBTAINED' named entity 'CHAINS' named entity 'CELLULAR' named entity 'PROTEIN G' named entity 'COMPARISON' named entity 'REINFORCEMENT' named entity 'CONTAINING' named entity 'PROTEIN SCIENCE' named entity 'DEMONSTRATED' named entity 'EFFECTIVE' named entity 'LIMITED' named entity 'FUSED TO' named entity 'BACKBONE' named entity 'CATENANES' named entity 'ARRANGEMENT' named entity 'CATENANE' named entity 'IN VIVO' named entity 'TOPOLOGY' named entity 'UNCONVENTIONAL' named entity 'PROTEINS' named entity 'GUIDES' named entity 'PROTEIN TOPOLOGY' named entity 'VARIETY' named entity 'REVEALS' named entity 'USING' named entity 'STABILITY' named entity 'FUNCTION' named entity 'DOMAIN' named entity 'MUCH' named entity 'PROTEIN DOMAINS' named entity 'MELTING POINT' named entity 'REPORT' named entity 'TRYPSIN DIGESTION'

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