Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly

EMBO Reports

Volumn 4, Issue 10, 2003, Pages 959-963

  Fehlker, Marion ^a   Wendler, Petra ^a   Lehmann, Andrea ^a   Enenkel, Cordula ^a  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BLM3 PROTEIN; CORE PROTEIN; NUCLEAR PROTEIN; PROTEASOME; PROTEIN PRECURSOR; UMP1 PROTEIN; UNCLASSIFIED DRUG; PROTEIN BLM3;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; FRACTIONATION; FUNGAL CELL; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN METABOLISM; PROTEIN PROCESSING; SACCHAROMYCES CEREVISIAE; WILD TYPE; ENZYME DEGRADATION; ENZYME MECHANISM; FUNGAL STRAIN; GEL ELECTROPHORESIS; GENOTYPE; YEAST;

CYSTEINE ENDOPEPTIDASES; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; MULTIENZYME COMPLEXES; NUCLEAR PROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN PRECURSORS; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBCELLULAR FRACTIONS;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0242522904     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.embor938     Document Type: Article

References (14)

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. Enenkel, C., Lehmann, A. & Kloetzel, P.M. (1998) Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast. EMBO J., 17, 6144-6154.
3. Evans Febres, D., Pramanik, A., Caton, M., Doherty, K., McKoy, J., Garcia, E., Alejo, W. & Moore, C.W. (2001) The novel BLM3 gene encodes a protein that protects against lethal effects of oxidative damage. Cell. Mol. Biol., 47, 1149-1162.
4. Frentzel, S., Pesold-Hurt, B., Seelig, A. & Kloetzel, P.M. (1994). 20S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins takes place in 13-16S preproteasome complexes. J. Mol. Biol., 236, 975-981.
5. Gavin, A.-C. et al. (2002). Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature, 415, 141-147.
6. Glickman, M.H. & Maytal, V. (2002) Regulating the 26S proteasome. Curr. Top. Microbiol. Immunol., 268, 43-72.
7. Heinemeyer, W. (2000) in Proteasomes: the World of Regulatory Proteolysis (eds Hilt, W. & Wolf, D.H.), 48-70 (Eurekah.com/Landes Biosciences Publ. Co., Georgetown, Texas, USA).
8. Jäger, S., Groll, M., Huber, R., Wolf, D.H. & Heinemeyer, W. (1999) Proteasome β-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function. J. Mol. Biol., 291, 997-1013.
9. Krüger, E., Kloetzel, P.-M. & Enenkel, C. (2001) 20S proteasome biogenesis. Biochimie, 83, 1-5.
10. Lehmann, A., Janek, K., Braun, B., Kloetzel, P.-M. & Enenkel, C. (2002). 20S proteasomes are imported as precursor complexes into the nucleus of yeast. J. Mol. Biol., 317, 401-413.
11. Ramos, P.C., Hockendorff, J., Johnson, E.S., Varshavsky, A. & Dohmen, R.J. (1998) Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell, 92, 489-499.
12. Russell, S.J., Steger, K.A. & Johnston, S.A. (1999) Subcellular localization, stoichiometry, and protein levels of 26S proteasome subunits in yeast. J. Biol. Chem., 274, 21943-21952.
13. Ustrell, V., Hoffman, L., Pratt, G. & Rechsteiner, M. (2002) PA200, a nuclear proteasome activator involved in DNA repair. EMBO J., 21, 3516-3525.
14. Wilkinson, C.R., Wallace, M., Morphew, M., Perry, P., Allshire, R., Javerzat, J.P., McIntosh, J.R. & Gordon, C. (1998). Localization of the 26S proteasome during mitosis and meiosis in fission yeast. EMBO J., 17, 6465-6476.