Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups

Carlos A. Castañeda; Jia Liu; Tanuja R. Kashyap; Rajesh K. Singh; David Fushman; T. Ashton Cropp

doi:10.1039/c0cc04868b

Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups

Carlos A. Castañeda, Jia Liu, Tanuja R. Kashyap, Rajesh K. Singh, David Fushman, T. Ashton Cropp

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

E2 enzymes catalyze the ATP-dependent polymerization of polyubiquitin chains which function as molecular signals in the regulation of numerous cellular processes. Here we present a method that uses genetically encoded unnatural amino acids to halt and re-start ubiquitin polymerization providing access to natural-linkage, precision-length ubiquitin chains that can be used for biochemical, structural, and dynamics studies.

Original language	English (US)
Pages (from-to)	2026-2028
Number of pages	3
Journal	Chemical Communications
Volume	47
Issue number	7
DOIs	https://doi.org/10.1039/c0cc04868b
State	Published - Feb 1 2011
Externally published	Yes

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Catalysis
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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abstract = "E2 enzymes catalyze the ATP-dependent polymerization of polyubiquitin chains which function as molecular signals in the regulation of numerous cellular processes. Here we present a method that uses genetically encoded unnatural amino acids to halt and re-start ubiquitin polymerization providing access to natural-linkage, precision-length ubiquitin chains that can be used for biochemical, structural, and dynamics studies.",

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AU - Castañeda, Carlos A.

AU - Liu, Jia

AU - Kashyap, Tanuja R.

AU - Singh, Rajesh K.

AU - Fushman, David

AU - Cropp, T. Ashton

PY - 2011/2/1

Y1 - 2011/2/1

N2 - E2 enzymes catalyze the ATP-dependent polymerization of polyubiquitin chains which function as molecular signals in the regulation of numerous cellular processes. Here we present a method that uses genetically encoded unnatural amino acids to halt and re-start ubiquitin polymerization providing access to natural-linkage, precision-length ubiquitin chains that can be used for biochemical, structural, and dynamics studies.

AB - E2 enzymes catalyze the ATP-dependent polymerization of polyubiquitin chains which function as molecular signals in the regulation of numerous cellular processes. Here we present a method that uses genetically encoded unnatural amino acids to halt and re-start ubiquitin polymerization providing access to natural-linkage, precision-length ubiquitin chains that can be used for biochemical, structural, and dynamics studies.

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Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups

Abstract

ASJC Scopus subject areas

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