Studying Weak and Dynamic Interactions of Posttranslationally
Modified Proteins using Expressed Protein Ligation

J 2014

Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation

TRIPSIANES, Konstantinos, Nam K. CHU, Anders FRIBERG, Michael SATTLER, Christian F. W. BECKER et. al.

Basic information

Original name

Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation

Authors

TRIPSIANES, Konstantinos (300 Greece, guarantor, belonging to the institution), Nam K. CHU (36 Australia), Anders FRIBERG (276 Germany), Michael SATTLER (276 Germany) and Christian F. W. BECKER (36 Australia)

Edition

ACS CHEMICAL BIOLOGY, Washington D.C. AMER CHEMICAL SOC, 2014, 1554-8929

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 5.331

RIV identification code

RIV/00216224:14740/14:00077435

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1021/cb400723j

UT WoS

000331927000005

Keywords in English

SMN TUDOR DOMAIN; RESOLUTION X-RAY; CHEMICAL-SYNTHESIS; ARGININE RESIDUES; SEMISYNTHESIS; PHOTOCONTROL; BINDING; SITE

Abstract

V originále

Many cellular processes are regulated by posttranslational modifications that are recognized by specific domains in protein binding partners. These interactions are often weak, thus allowing a highly dynamic and combinatorial regulatory network of protein-protein interactions. We report an efficient strategy that overcomes challenges in structural analysis of such a weak transient interaction between the Tudor domain of the Survival of Motor Neuron (SMN) protein and symmetrically dimethylated arginine (sDMA). The posttranslational modification is chemically introduced and covalently linked to the effector module by a one-pot expressed protein ligation (EPL) procedure also enabling segmental incorporation of NMR-active isotopes for structural analysis. Covalent coupling of the two interacting moieties shifts the equilibrium to the bound state, and stoichiometric interactions are formed even for low affinity interactions. Our approach should enable the structural analysis of weak interactions by NMR or X-ray crystallography to better understand the role of posttranslational modifications in dynamic biological processes.

Citovat

TRIPSIANES, Konstantinos, Nam K. CHU, Anders FRIBERG, Michael SATTLER and Christian F. W. BECKER. Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation. ACS CHEMICAL BIOLOGY. Washington D.C.: AMER CHEMICAL SOC, 2014, vol. 9, No 2, p. 347-352. ISSN 1554-8929. Available from: https://dx.doi.org/10.1021/cb400723j.

@article{1210376,
   author = {Tripsianes, Konstantinos and Chu, Nam K. and Friberg, Anders and Sattler, Michael and Becker, Christian F. W.},
   article_location = {Washington D.C.},
   article_number = {2},
   doi = {http://dx.doi.org/10.1021/cb400723j},
   keywords = {SMN TUDOR DOMAIN; RESOLUTION X-RAY; CHEMICAL-SYNTHESIS; ARGININE RESIDUES; SEMISYNTHESIS; PHOTOCONTROL; BINDING; SITE},
   language = {eng},
   issn = {1554-8929},
   journal = {ACS CHEMICAL BIOLOGY},
   title = {Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation},
   url = {http://pubs.acs.org/doi/abs/10.1021/cb400723j},
   volume = {9},
   year = {2014}
}

TY  - JOUR
ID  - 1210376
AU  - Tripsianes, Konstantinos - Chu, Nam K. - Friberg, Anders - Sattler, Michael - Becker, Christian F. W.
PY  - 2014
TI  - Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation
JF  - ACS CHEMICAL BIOLOGY
VL  - 9
IS  - 2
SP  - 347-352
EP  - 347-352
PB  - AMER CHEMICAL SOC
SN  - 15548929
KW  - SMN TUDOR DOMAIN
KW  - RESOLUTION X-RAY
KW  - CHEMICAL-SYNTHESIS
KW  - ARGININE RESIDUES
KW  - SEMISYNTHESIS
KW  - PHOTOCONTROL
KW  - BINDING
KW  - SITE
UR  - http://pubs.acs.org/doi/abs/10.1021/cb400723j
L2  - http://pubs.acs.org/doi/abs/10.1021/cb400723j
N2  - Many cellular processes are regulated by posttranslational modifications that are recognized by specific domains in protein binding partners. These interactions are often weak, thus allowing a highly dynamic and combinatorial regulatory network of protein-protein interactions. We report an efficient strategy that overcomes challenges in structural analysis of such a weak transient interaction between the Tudor domain of the Survival of Motor Neuron (SMN) protein and symmetrically dimethylated arginine (sDMA). The posttranslational modification is chemically introduced and covalently linked to the effector module by a one-pot expressed protein ligation (EPL) procedure also enabling segmental incorporation of NMR-active isotopes for structural analysis. Covalent coupling of the two interacting moieties shifts the equilibrium to the bound state, and stoichiometric interactions are formed even for low affinity interactions. Our approach should enable the structural analysis of weak interactions by NMR or X-ray crystallography to better understand the role of posttranslational modifications in dynamic biological processes.
ER  -

TRIPSIANES, Konstantinos, Nam K. CHU, Anders FRIBERG, Michael SATTLER and Christian F. W. BECKER. Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation. \textit{ACS CHEMICAL BIOLOGY}. Washington D.C.: AMER CHEMICAL SOC, 2014, vol.~9, No~2, p.~347-352. ISSN~1554-8929. Available from: https://dx.doi.org/10.1021/cb400723j.

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