Structural Features of the 26 S Proteasome Complex

Peters, Jan‐Michael; Cejka, Zdenka; Harris, J. Robin; Kleinschmidt, Jürgen A.; Baumeister, Wolfgang

doi:10.1006/jmbi.1993.1646

Cited by 242 publications

(145 citation statements)

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“…The other subunits indicated were positioned by chemical crosslinking (solid lines) as shown in Fig. 4. some clearly reflects the 2-fold symmetry (46). This implies an alignment of the activator along the diameter approximately vertical to the 2-fold axis of the 20S proteasome-i.e., along a line from C2 to C3͞C9.…”

Section: Discussionmentioning

confidence: 91%

Subunit arrangement in the human 20S proteasome

Köpp

Hendil

Dahlmann

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

110

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In human 20S proteasomes two copies of each of seven different ␣-type and seven different ␤-type subunits are assembled to form a stack of four sevenmembered rings, giving the general structure ␣ 1-7 , ␤ 1-7 , ␤ 1-7 , ␣ 1-7 . By means of immunoelectron microscopy and chemical crosslinking of neighboring subunits, we have determined the positions of the individual subunits in the proteasome. The topography shows that for the trypsin-like, the chymotrypsin-like, and the postglutamyl cleaving activities, the pairs of ␤ type subunits, which are thought to form active sites, are nearest neighbors.

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Section: Discussionmentioning

confidence: 91%

Subunit arrangement in the human 20S proteasome

Köpp

Hendil

Dahlmann

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

110

View full text Add to dashboard Cite

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“…The eukaryotic 20S core is composed of 14 subunits and forms a barrel-shaped structure of four seven-membered rings (Peters et al 1993). A functionally and structurally similar 20S particle is present in archaebacteria.…”

Section: The Proteasomal Regulatory Proteinsmentioning

confidence: 99%

The Evolution of the Conserved ATPase Domain (CAD): Reconstructing the History of an Ancient Protein Module

Swaffield

Purugganan

1997

J Mol Evol

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Abstract. The AAA proteins (ATPases Associated with a variety of cellular Activities) are found in eubacterial, archaebacterial, and eukaryotic species and participate in a large number of cellular processes, including protein degradation, vesicle fusion, cell cycle control, and cellular secretory processes. The AAA proteins are characterized by the presence of a 230 to 250-amino acid ATPase domain referred to as the Conserved ATPase Domain or CAD. Phylogenetic analysis of 133 CAD sequences from 38 species reveal that AAA CADs are organized into discrete groups that are related not only in structure but in cellular function. Evolutionary analyses also indicate that the CAD was present in the last common ancestor of eubacteria, archaebacteria, and eukaryotes. The eubacterial CADs are found in metalloproteases, while CAD-containing proteins in the archaebacterial and eukaryotic lineages appear to have diversified by a series of gene duplication events that lead to the establishment of different functional AAA proteins, including proteasomal regulatory, NSF/Sec, and Pas proteins. The phylogeny of the CADs provides the basis for establishing the patterns of evolutionary change that characterize the AAA proteins.

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“…Recently, a high-molecularweight complex containing Yme1p has been identified, as well as a complex involving both Afg3p and Rca1p (Arlt et al 1996;Thomas Langer, personal communication). Formation of homo-multimers is also seen with other members of the AAA family (Peters et al 1990(Peters et al , 1993Whiteheart et al 1994;Fröhlich et al 1995) and may be a common feature of these proteins. Figure 1 shows the location and (putative) quaternary structure of the mitochondrial proteases the yeast genes of which have been cloned.…”

Section: Are All Mitochondrial Atp-dependent Proteases Multimers?mentioning

confidence: 89%