Disulfide engineering to map subunit interactions in the proteasome and other macromolecular complexes

Methods in Molecular Biology

Volumn 832, Issue , 2012, Pages 349-362

  Hochstrasser, Mark ^a   Funakoshi, Minoru ^a,b  

^a YALE UNIVERSITY   (United States)

^b OKAYAMA UNIVERSITY   (Japan)

Author keywords

Disulfide engineering; Immunoblotting; Nondenaturing polyacrylamide gel electrophoresis (native PAGE); Proteasome; Saccharomyces cerevisiae; Site directed mutagenesis; Substrate overlay; Yeast

Indexed keywords

ATP DEPENDENT 26S PROTEASE; DISULFIDE; PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CHEMISTRY; IMMUNOBLOTTING; METABOLISM; METHODOLOGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN QUATERNARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; IMMUNOBLOTTING; MUTAGENESIS, SITE-DIRECTED; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN STRUCTURE, QUATERNARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 84858246318     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-474-2_24     Document Type: Article

References (18)

1. Chen P, Hochstrasser M (1996) Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86 :961-972.
2. Arendt CS, Hochstrasser M (1997) Identifi cation of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Natl. Acad. Sci. U.S.A. 94 :7156-7161.
3. Velichutina I, Connerly PL, Arendt CS et al (2004) Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. Embo J 23 :500-510.
4. Kusmierczyk AR, Kunjappu MJ, Funakoshi M, Hochstrasser M (2008) A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nat Struct Mol Biol 15 :237-244.
5. Tomko RJ, Jr, Funakoshi M, Schneider K et al (2010) Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: Implications for proteasome structure and assembly. Mol Cell 38 :393-403.
6. Hochstrasser M (1996) Ubiquitin-dependent protein degradation. Annual Review of Genetics 30 :405-439.
7. Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiological Reviews 82 :373-428.
8. Pickart CM, Cohen RE (2004) Proteasomes and their kin: Proteases in the machine age. Nat Rev Mol Cell Biol 5 :177-187.
9. Marques AJ, Palanimurugan R, Matias AC et al (2009) Catalytic mechanism and assembly of the proteasome. Chem Rev 109 :1509-1536.
10. Chen P, Hochstrasser M (1995) Biogenesis, structure, and function of the yeast 20S proteasome. EMBO J. 14 :2620-2630.
11. Groll M, Ditzel L, Löwe J et al (1997) Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386 :463-471.
12. Fu H, Reis N, Lee Y et al (2001) Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO Journal 20 :7096-7107.
13. Zhang F, Hu M, Tian G et al (2009) Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii . Mol Cell 34 :473-484.
14. Djuranovic S, Hartmann MD, Habeck M et al (2009) Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases. Mol Cell 34 :580-590.
15. Verma R, Chen S, Feldman R et al (2000) Proteasomal proteomics: Identifi cation of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affi nity-purifi ed proteasomes. Mol Biol Cell 11 :3425-3439.
16. Hough R, Pratt G, Rechsteiner M (1987) Purifi cation of two high molecular weight proteases in rabbit reticulocyte lysate. J. Biol. Chem. 262 :8303-8313.
17. Glickman MH, Rubin DM, Fried VA, Finley D (1998) The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18 :3149-3162.
18. Elsasser S, Schmidt M, Finley D (2005) Characterization of the proteasome using native gel electrophoresis. Methods Enzymol 398 :353-363.