Structural biology of the DJ-1 superfamily

Nathan Smith, Mark A. Wilson

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Citations (Scopus)

Abstract

The DJ-1 (also called the DJ-1/PfpI, ThiJ/PfpI, or DJ-1/ThiJ/PfpI) superfamily is a structural and functional diverse group of proteins that are present in most organisms. Many of these proteins remain poorly characterized at the biochemical level, but include some known chaperones, proteases, and various stress response proteins that remain mechanistically mysterious. This chapter outlines what is known from a structural perspective about the cellular and biochemical functions of many of these proteins from distinct clades of the superfamily in several organisms. In humans, DJ-1 appears to function primarily as a redox-responsive protein that may act as a sensor for imbalances in cellular redox state. Because mutations in human DJ-1 cause certain types of heritable Parkinson’s disease, the role of oxidative posttranslational modifications and pathogenic mutations in human DJ-1 is emphasized in the latter sections of this chapter.

Original languageEnglish (US)
Title of host publicationAdvances in Experimental Medicine and Biology
PublisherSpringer New York LLC
Pages5-24
Number of pages20
DOIs
StatePublished - Jan 1 2017

Publication series

NameAdvances in Experimental Medicine and Biology
Volume1037
ISSN (Print)0065-2598
ISSN (Electronic)2214-8019

Fingerprint

Oxidation-Reduction
Proteins
Mutation
Post Translational Protein Processing
Heat-Shock Proteins
Parkinson Disease
Peptide Hydrolases
Functional groups
Sensors

Keywords

  • Chaperone
  • Cysteine oxidation
  • DJ-1
  • Glyoxalase
  • Oxidative stress
  • Protease
  • Structural biology
  • Sulfinic acid
  • Sulfonic acid
  • X-ray crystallography

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Smith, N., & Wilson, M. A. (2017). Structural biology of the DJ-1 superfamily. In Advances in Experimental Medicine and Biology (pp. 5-24). (Advances in Experimental Medicine and Biology; Vol. 1037). Springer New York LLC. https://doi.org/10.1007/978-981-10-6583-5_2

Structural biology of the DJ-1 superfamily. / Smith, Nathan; Wilson, Mark A.

Advances in Experimental Medicine and Biology. Springer New York LLC, 2017. p. 5-24 (Advances in Experimental Medicine and Biology; Vol. 1037).

Research output: Chapter in Book/Report/Conference proceedingChapter

Smith, N & Wilson, MA 2017, Structural biology of the DJ-1 superfamily. in Advances in Experimental Medicine and Biology. Advances in Experimental Medicine and Biology, vol. 1037, Springer New York LLC, pp. 5-24. https://doi.org/10.1007/978-981-10-6583-5_2
Smith N, Wilson MA. Structural biology of the DJ-1 superfamily. In Advances in Experimental Medicine and Biology. Springer New York LLC. 2017. p. 5-24. (Advances in Experimental Medicine and Biology). https://doi.org/10.1007/978-981-10-6583-5_2
Smith, Nathan ; Wilson, Mark A. / Structural biology of the DJ-1 superfamily. Advances in Experimental Medicine and Biology. Springer New York LLC, 2017. pp. 5-24 (Advances in Experimental Medicine and Biology).
@inbook{d261feb999ac428a97cc3699fd20818a,
title = "Structural biology of the DJ-1 superfamily",
abstract = "The DJ-1 (also called the DJ-1/PfpI, ThiJ/PfpI, or DJ-1/ThiJ/PfpI) superfamily is a structural and functional diverse group of proteins that are present in most organisms. Many of these proteins remain poorly characterized at the biochemical level, but include some known chaperones, proteases, and various stress response proteins that remain mechanistically mysterious. This chapter outlines what is known from a structural perspective about the cellular and biochemical functions of many of these proteins from distinct clades of the superfamily in several organisms. In humans, DJ-1 appears to function primarily as a redox-responsive protein that may act as a sensor for imbalances in cellular redox state. Because mutations in human DJ-1 cause certain types of heritable Parkinson’s disease, the role of oxidative posttranslational modifications and pathogenic mutations in human DJ-1 is emphasized in the latter sections of this chapter.",
keywords = "Chaperone, Cysteine oxidation, DJ-1, Glyoxalase, Oxidative stress, Protease, Structural biology, Sulfinic acid, Sulfonic acid, X-ray crystallography",
author = "Nathan Smith and Wilson, {Mark A.}",
year = "2017",
month = "1",
day = "1",
doi = "10.1007/978-981-10-6583-5_2",
language = "English (US)",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer New York LLC",
pages = "5--24",
booktitle = "Advances in Experimental Medicine and Biology",

}

TY - CHAP

T1 - Structural biology of the DJ-1 superfamily

AU - Smith, Nathan

AU - Wilson, Mark A.

PY - 2017/1/1

Y1 - 2017/1/1

N2 - The DJ-1 (also called the DJ-1/PfpI, ThiJ/PfpI, or DJ-1/ThiJ/PfpI) superfamily is a structural and functional diverse group of proteins that are present in most organisms. Many of these proteins remain poorly characterized at the biochemical level, but include some known chaperones, proteases, and various stress response proteins that remain mechanistically mysterious. This chapter outlines what is known from a structural perspective about the cellular and biochemical functions of many of these proteins from distinct clades of the superfamily in several organisms. In humans, DJ-1 appears to function primarily as a redox-responsive protein that may act as a sensor for imbalances in cellular redox state. Because mutations in human DJ-1 cause certain types of heritable Parkinson’s disease, the role of oxidative posttranslational modifications and pathogenic mutations in human DJ-1 is emphasized in the latter sections of this chapter.

AB - The DJ-1 (also called the DJ-1/PfpI, ThiJ/PfpI, or DJ-1/ThiJ/PfpI) superfamily is a structural and functional diverse group of proteins that are present in most organisms. Many of these proteins remain poorly characterized at the biochemical level, but include some known chaperones, proteases, and various stress response proteins that remain mechanistically mysterious. This chapter outlines what is known from a structural perspective about the cellular and biochemical functions of many of these proteins from distinct clades of the superfamily in several organisms. In humans, DJ-1 appears to function primarily as a redox-responsive protein that may act as a sensor for imbalances in cellular redox state. Because mutations in human DJ-1 cause certain types of heritable Parkinson’s disease, the role of oxidative posttranslational modifications and pathogenic mutations in human DJ-1 is emphasized in the latter sections of this chapter.

KW - Chaperone

KW - Cysteine oxidation

KW - DJ-1

KW - Glyoxalase

KW - Oxidative stress

KW - Protease

KW - Structural biology

KW - Sulfinic acid

KW - Sulfonic acid

KW - X-ray crystallography

UR - http://www.scopus.com/inward/record.url?scp=85034864812&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85034864812&partnerID=8YFLogxK

U2 - 10.1007/978-981-10-6583-5_2

DO - 10.1007/978-981-10-6583-5_2

M3 - Chapter

C2 - 29147900

AN - SCOPUS:85034864812

T3 - Advances in Experimental Medicine and Biology

SP - 5

EP - 24

BT - Advances in Experimental Medicine and Biology

PB - Springer New York LLC

ER -