Object's details: Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein
Creator:
Lenarčič Živković, Martina;
Zaręba-Kozioł, Monika;
Zhukova, Liliya;
Poznański, Jarosław;
Zhukov, Igor;
Wysłouch-Cieszyńska, Aleksandra
Description:
S100A1 is a member of the Ca2+-binding S100 protein family. It is expressed in brain and heart tissue, where it plays a crucial role as a modulator of Ca2+ homeostasis, energy metabolism, neurotransmitter release, and contractile performance. Biological effects of S100A1 have been attributed to its direct interaction with a variety of target proteins. The (patho)physiological relevance of S100A1 makes it an important molecular target for future therapeutic intervention. S-Nitrosylation is a post-translational modification of proteins, which plays a role in cellular signal transduction under physiological and pathological conditions. In this study, we confirmed that S100A1 protein is endogenously modified by Cys85 S-nitrosylation in PC12 cells, which are a well established model system for studying S100A1 function. We used isothermal calorimetry to show that S-nitrosylation facilitates the formation of Ca2+-loaded S100A1 at physiological ionic strength conditions. To establish the unique influence of the S-nitroso group, our study describes high resolution three-dimensional structures of human apo-S100A1 protein with the Cys85 thiol group in reduced and S-nitrosylated states. Solution structures of the proteins are based on NMR data obtained at physiological ionic strength. Comparative analysis shows that S-nitrosylation fine tunes the overall architecture of S100A1 protein. Although the typical S100 protein intersubunit four-helix bundle is conserved upon S-nitrosylation, the conformation of S100A1 protein is reorganized at the sites most important for target recognition (i.e. the C-terminal helix and the linker connecting two EF-hand domains). In summary, this study discloses cysteine S-nitrosylation as a new factor responsible for increasing functional diversity of S100A1 and helps explain the role of S100A1 as a Ca2+ signal transmitter sensitive to NO/redox equilibrium within cells.
Object availability:
free access
Date:
2012.11.23
Type:
Article;
PeerReviewed
Language:
English;
eng
Format:
text/html
Publisher:
American Society for Biochemistry and Molecular Biology
Relation: http://eprints.ibb.waw.pl/526 ;http://www.jbc.org/content/287/48/40457.full ;
10.1074/jbc.M112.418392
Subject:
QC Physics;
QD Chemistry
Identifier: http://eprints.ibb.waw.pl/526/1/40457.long ;
Lenarčič Živković, Martina and Zaręba-Kozioł, Monika and Zhukova, Liliya and Poznański, Jarosław and Zhukov, Igor and Wysłouch-Cieszyńska, Aleksandra (2012) Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein. The Journal of biological chemistry, 287 (48). pp. 40457-40470. ISSN 1083-351X
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Similar objects

Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein

Date:2012.11.23

Type:other

Structural Analysis of the SANT/Myb Domain of FLASH and YARP Proteins and Their Complex with the C-Terminal Fragment of NPAT by NMR Spectroscopy and Computer Simulations

Date:2020.07.24

Type:other

Spectroscopic and thermodynamic determination of three distinct binding sites for Co(II) ions in human serum albumin.

Creator:Sokołowska, Magdalena | Wszelaka-Rylik, Małgorzata | Poznański, Jarosław | Bal, Wojciech

Date:2009

Type:other

Revisiting Mitochondrial pH with an Improved Algorithm for Calibration of the Ratiometric 5(6)-carboxy-SNARF-1 Probe Reveals Anticooperative Reaction with H+ Ions and Warrants Further Studies of Organellar pH

Date:2016.08

Type:other

Determining the Identity of Nucleotides and the Energy of Binding of tRNAs to Their Aminoacyl-tRNA Synthetases Using a Simple Logistic Model

Creator:Pawłowski, Piotr H | Zielenkiewicz, Piotr

Date:2024.10.18

Type:other

Non-specific clustering of histidine tagged green fluorescent protein mediated by surface interactions: the collective effect in the protein-adsorption behaviour

Creator:Sobieściak, Tomasz D. | Zielenkiewicz, Piotr

Date:2013

Type:other

Pentetic acid (DPTA) Cu(II) monolayer deposited on gold electrode—The base of biosensors for electrochemical screening of kinase JAK2 and potential inhibitor interactions

Date:2014.06

Type:other

Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes.

Date:2014.12

Type:other

Federacja Bibliotek Cyfrowych

Object's details: Post-translational S-Nitrosylation Is an Endogenous Factor Fine Tuning the Properties of Human S100A1 Protein

Description

Similar objects