1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

Chingakham R. Singh; Scott Lovell; Nurjahan Mehzabeen; Wasimul Q. Chowdhury; Kevin P. Battaile; Jeroen Roelofs

doi:10.1107/S2053230X14003884

1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

Chingakham R. Singh
, Scott Lovell
, Nurjahan Mehzabeen
, Wasimul Q. Chowdhury
, Kevin P. Battaile
, Jeroen Roelofs

Biology

Kansas State University
University of Kansas
IMCA-CAT Hauptman-Woodward Medical Research Institute

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

6 Scopus citations

12 Downloads (Pure)

Abstract

The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.

Original language	English
Pages (from-to)	418-423
Number of pages	6
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	70
Issue number	4
DOIs	https://doi.org/10.1107/S2053230X14003884
State	Published - Mar 24 2014

Scopus Subject Areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

Keywords

Nas2
PDZ domain
chaperones
proteasome
Amino Acid Sequence
Molecular Chaperones/chemistry
Saccharomyces cerevisiae Proteins/chemistry
Crystallization
Models, Molecular
Molecular Sequence Data
Sequence Homology, Amino Acid
Crystallography, X-Ray/methods
Saccharomyces cerevisiae/metabolism
Adenosine Triphosphatases/chemistry
PDZ Domains
Protein Conformation

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10.1107/S2053230X14003884

Cite this

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title = "1.15 {\AA} resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain",

abstract = "The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 {\AA} resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.",

keywords = "Nas2, PDZ domain, chaperones, proteasome, Amino Acid Sequence, Molecular Chaperones/chemistry, Saccharomyces cerevisiae Proteins/chemistry, Crystallization, Models, Molecular, Molecular Sequence Data, Sequence Homology, Amino Acid, Crystallography, X-Ray/methods, Saccharomyces cerevisiae/metabolism, Adenosine Triphosphatases/chemistry, PDZ Domains, Protein Conformation",

author = "Singh, \{Chingakham R.\} and Scott Lovell and Nurjahan Mehzabeen and Chowdhury, \{Wasimul Q.\} and Battaile, \{Kevin P.\} and Jeroen Roelofs",

year = "2014",

month = mar,

day = "24",

doi = "10.1107/S2053230X14003884",

language = "English",

volume = "70",

pages = "418--423",

journal = "Acta Crystallographica Section F: Structural Biology Communications",

issn = "2053-230X",

publisher = "John Wiley and Sons Ltd",

number = "4",

}

TY - JOUR

T1 - 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

AU - Singh, Chingakham R.

AU - Lovell, Scott

AU - Mehzabeen, Nurjahan

AU - Chowdhury, Wasimul Q.

AU - Battaile, Kevin P.

AU - Roelofs, Jeroen

PY - 2014/3/24

Y1 - 2014/3/24

N2 - The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.

AB - The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.

KW - Nas2

KW - PDZ domain

KW - chaperones

KW - proteasome

KW - Amino Acid Sequence

KW - Molecular Chaperones/chemistry

KW - Saccharomyces cerevisiae Proteins/chemistry

KW - Crystallization

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Sequence Homology, Amino Acid

KW - Crystallography, X-Ray/methods

KW - Saccharomyces cerevisiae/metabolism

KW - Adenosine Triphosphatases/chemistry

KW - PDZ Domains

KW - Protein Conformation

UR - https://www.scopus.com/pages/publications/84905448136

U2 - 10.1107/S2053230X14003884

DO - 10.1107/S2053230X14003884

M3 - Article

C2 - 24699731

SN - 2053-230X

VL - 70

SP - 418

EP - 423

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - 4

ER -

1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

Abstract

Scopus Subject Areas

Keywords

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