Structural and biochemical analyses of the eukaryotic heat shock locus v (HslV) from Trypanosoma brucei

Kwang Hoon Sung, So Yeon Lee, Hyun Kyu Song

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Background: A eukaryotic HslV (TbHslV) protease and two potential HslU (TbHslU1 and TbHslU2) ATPases have been isolated from Trypanosoma brucei. Results: We determined the crystal structure of TbHslV at 2.4 Å resolution. Only TbHslU2 activated TbHslV protease activity. Conclusion: A key tyrosine residue in TbHslU2 required for activating TbHslV was identified. Significance: This study lays the groundwork for understanding the eukaryotic HslVU system.

Original languageEnglish
Pages (from-to)23234-23243
Number of pages10
JournalJournal of Biological Chemistry
Volume288
Issue number32
DOIs
Publication statusPublished - 2013 Aug 9

Fingerprint

Trypanosoma brucei brucei
Shock
Peptide Hydrolases
Hot Temperature
Tyrosine
Adenosine Triphosphatases
Crystal structure

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Structural and biochemical analyses of the eukaryotic heat shock locus v (HslV) from Trypanosoma brucei. / Sung, Kwang Hoon; Lee, So Yeon; Song, Hyun Kyu.

In: Journal of Biological Chemistry, Vol. 288, No. 32, 09.08.2013, p. 23234-23243.

Research output: Contribution to journalArticle

@article{238582e24790429fbeee72b55887b21b,
title = "Structural and biochemical analyses of the eukaryotic heat shock locus v (HslV) from Trypanosoma brucei",
abstract = "Background: A eukaryotic HslV (TbHslV) protease and two potential HslU (TbHslU1 and TbHslU2) ATPases have been isolated from Trypanosoma brucei. Results: We determined the crystal structure of TbHslV at 2.4 {\AA} resolution. Only TbHslU2 activated TbHslV protease activity. Conclusion: A key tyrosine residue in TbHslU2 required for activating TbHslV was identified. Significance: This study lays the groundwork for understanding the eukaryotic HslVU system.",
author = "Sung, {Kwang Hoon} and Lee, {So Yeon} and Song, {Hyun Kyu}",
year = "2013",
month = "8",
day = "9",
doi = "10.1074/jbc.M113.484832",
language = "English",
volume = "288",
pages = "23234--23243",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "32",

}

TY - JOUR

T1 - Structural and biochemical analyses of the eukaryotic heat shock locus v (HslV) from Trypanosoma brucei

AU - Sung, Kwang Hoon

AU - Lee, So Yeon

AU - Song, Hyun Kyu

PY - 2013/8/9

Y1 - 2013/8/9

N2 - Background: A eukaryotic HslV (TbHslV) protease and two potential HslU (TbHslU1 and TbHslU2) ATPases have been isolated from Trypanosoma brucei. Results: We determined the crystal structure of TbHslV at 2.4 Å resolution. Only TbHslU2 activated TbHslV protease activity. Conclusion: A key tyrosine residue in TbHslU2 required for activating TbHslV was identified. Significance: This study lays the groundwork for understanding the eukaryotic HslVU system.

AB - Background: A eukaryotic HslV (TbHslV) protease and two potential HslU (TbHslU1 and TbHslU2) ATPases have been isolated from Trypanosoma brucei. Results: We determined the crystal structure of TbHslV at 2.4 Å resolution. Only TbHslU2 activated TbHslV protease activity. Conclusion: A key tyrosine residue in TbHslU2 required for activating TbHslV was identified. Significance: This study lays the groundwork for understanding the eukaryotic HslVU system.

UR - http://www.scopus.com/inward/record.url?scp=84881398584&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84881398584&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.484832

DO - 10.1074/jbc.M113.484832

M3 - Article

C2 - 23818520

AN - SCOPUS:84881398584

VL - 288

SP - 23234

EP - 23243

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 32

ER -