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Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation

Kurimoto, Eiji (author)
Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
Satoh, Tadashi (author)
Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;JST, PRESTO, Mizuho Ku, Nagoya, Aichi 4678603, Japan.
Ito, Yuri (author)
Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
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Ishihara, Eri (author)
Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan.
Okamoto, Kenta (author)
Uppsala universitet,Molekylär biofysik,Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan
Yagi-Utsumi, Maho (author)
Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;Natl Inst Nat Sci, Okazaki Inst Integrat Biosci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.;Natl Inst Nat Sci, Inst Mol Sci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.
Tanaka, Keiji (author)
Tokyo Metropolitan Inst Med Sci, Lab Prot Metab, Setagaya Ku, Tokyo 1568506, Japan.
Kato, Koichi (author)
Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;Natl Inst Nat Sci, Okazaki Inst Integrat Biosci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.;Natl Inst Nat Sci, Inst Mol Sci, 5-1 Higashiyama, Okazaki, Aichi 4448787, Japan.
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Meijo Univ, Fac Pharm, Tempaku Ku, 150 Yagotoyama, Nagoya, Aichi 4688503, Japan Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan.;JST, PRESTO, Mizuho Ku, Nagoya, Aichi 4678603, Japan. (creator_code:org_t)
2017-03-16
2017
English.
In: Protein Science. - : WILEY. - 0961-8368 .- 1469-896X. ; 26:5, s. 1080-1085
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • The 26S proteasome is a large protein complex, responsible for degradation of ubiquinated proteins in eukaryotic cells. Eukaryotic proteasome formation is a highly ordered process that is assisted by several assembly chaperones. The assembly of its catalytic 20S core particle depends on at least five proteasome-specific chaperones, i.e., proteasome-assembling chaperons 1-4 (PAC1-4) and proteasome maturation protein (POMP). The orthologues of yeast assembly chaperones have been structurally characterized, whereas most mammalian assembly chaperones are not. In the present study, we determined a crystal structure of human PAC4 at 1.90-angstrom resolution. Our crystallographic data identify a hydrophobic surface that is surrounded by charged residues. The hydrophobic surface is complementary to that of its binding partner, PAC3. The surface also exhibits charge complementarity with the proteasomal 4-5 subunits. This will provide insights into human proteasome-assembling chaperones as potential anticancer drug targets.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)

Keyword

assembly chaperone
crystal structure
PAC4
proteasome

Publication and Content Type

ref (subject category)
art (subject category)

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