Branding/Logomark minus Citation Combined Shape Icon/Bookmark-empty Icon/Copy Icon/Collection Icon/Close Copy 7 no author result Created with Sketch. Icon/Back Created with Sketch. Match!

Conversion of functionally undefined homopentameric protein PbaA into a proteasome activator by mutational modification of its C-terminal segment conformation

Published on Jan 1, 2018in Protein Engineering Design & Selection 1.98
· DOI :10.1093/protein/gzx066
Maho Yagi-Utsumi6
Estimated H-index: 6
(Nagoya City University),
Arunima Sikdar2
Estimated H-index: 2
(Graduate University for Advanced Studies)
+ 6 AuthorsKoichi Kato50
Estimated H-index: 50
(Nagoya City University)
Cite
  • References (18)
  • Citations (2)
Cite
References18
Newest
Published on Oct 1, 2014in Biochemical and Biophysical Research Communications 2.71
Arunima Sikdar2
Estimated H-index: 2
(Nagoya City University),
Tadashi Satoh15
Estimated H-index: 15
(Nagoya City University)
+ 1 AuthorsKoichi Kato50
Estimated H-index: 50
(Nagoya City University)
Abstract Formation of the eukaryotic proteasome is not a spontaneous process but a highly ordered process assisted by several assembly chaperones. In contrast, archaeal proteasome subunits can spontaneously assemble into an active form. Recent bioinformatic analysis identified the proteasome-assembly chaperone-like proteins, PbaA and PbaB, in archaea. Our previous study showed that the PbaB homotetramer functions as a proteasome activator through its tentacle-like C-terminal segments. However, a...
4 Citations Source Cite
Published on Jun 2, 2013in Annual Review of Biochemistry 26.92
Robert J. Tomko12
Estimated H-index: 12
(Yale University),
Mark Hochstrasser56
Estimated H-index: 56
(Yale University)
The eukaryotic ubiquitin-proteasome system is responsible for most aspects of regulatory and quality-control protein degradation in cells. Its substrates, which are usually modified by polymers of ubiquitin, are ultimately degraded by the 26S proteasome. This 2.6-MDa protein complex is separated into a barrel-shaped proteolytic 20S core particle (CP) of 28 subunits capped on one or both ends by a 19S regulatory particle (RP) comprising at least 19 subunits. The RP coordinates substrate recogniti...
182 Citations Source Cite
Published on Mar 21, 2013in PLOS ONE 2.78
Kentaro Kumoi2
Estimated H-index: 2
(Nagoya City University),
Tadashi Satoh15
Estimated H-index: 15
(Nagoya City University)
+ 7 AuthorsKoichi Kato50
Estimated H-index: 50
(Nagoya City University)
Assembly of the eukaryotic 20S proteasome is an ordered process involving several proteins operating as proteasome assembly factors including PAC1-PAC2 but archaeal 20S proteasome subunits can spontaneously assemble into an active cylindrical architecture. Recent bioinformatic analysis identified archaeal PAC1-PAC2 homologs PbaA and PbaB. However, it remains unclear whether such assembly factor-like proteins play an indispensable role in orchestration of proteasome subunits in archaea. We reveal...
13 Citations Source Cite
Published on May 1, 2011in Nature Structural & Molecular Biology 12.11
Andrew R. Kusmierczyk6
Estimated H-index: 6
(IUPUI: Indiana University – Purdue University Indianapolis),
Mary J. Kunjappu4
Estimated H-index: 4
(Yale University)
+ 1 AuthorsMark Hochstrasser56
Estimated H-index: 56
(Yale University)
Dedicated chaperones facilitate eukaryotic proteasome assembly, yet how they function remains largely unknown. Here we demonstrate that a yeast 20S proteasome assembly factor, Pba1–Pba2, requires a previously overlooked C-terminal HbYX (hydrophobic-tyrosine-X) motif for function. HbYX motifs in proteasome activators open the 20S proteasome entry pore, but Pba1–Pba2 instead binds inactive proteasomal precursors. We discovered an archaeal ortholog of this factor, here named PbaA, that also binds p...
47 Citations Source Cite
Published on Feb 1, 2009in Nature Reviews Molecular Cell Biology 43.35
Shigeo Murata46
Estimated H-index: 46
(UTokyo: University of Tokyo),
Hideki Yashiroda17
Estimated H-index: 17
(UTokyo: University of Tokyo),
Keiji Tanaka108
Estimated H-index: 108
The 26S proteasome is a large protein complex that consists of a catalytic 20S core and a 19S regulatory particle, each of which contains numerous subunits. Proteasome-dedicated chaperones guarantee the efficient and correct assembly of this degradation machine, which is essential for its function.
342 Citations Source Cite
Published on Jan 1, 2009
Keiji Tanaka108
Estimated H-index: 108
The proteasome is a highly sophisticated protease complex designed to carry out selective, efficient and processive hydrolysis of client proteins. It is known to collaborate with ubiquitin, which polymerizes to form a marker for regulated proteolysis in eukaryotic cells. The highly organized proteasome plays a prominent role in the control of a diverse array of basic cellular activities by rapidly and unidirectionally catalyzing biological reactions. Studies of the proteasome during the past qua...
229 Citations Source Cite
Published on Nov 1, 2008in Progress in Surface Science 8.76
Toshio Ando41
Estimated H-index: 41
(Kanazawa University),
Takayuki Uchihashi35
Estimated H-index: 35
(Kanazawa University),
Takeshi Fukuma24
Estimated H-index: 24
(Kanazawa University)
The atomic force microscope (AFM) has a unique capability of allowing the high-resolution imaging of biological samples on substratum surfaces in physiological solutions. Recent technological progress of AFM in biological research has resulted in remarkable improvements in both the imaging rate and the tip force acting on the sample. These improvements have enabled the direct visualization of dynamic structural changes and dynamic interactions occurring in individual biological macromolecules, w...
315 Citations Source Cite
Published on Sep 1, 2007in Molecular Cell 14.55
David M. Smith32
Estimated H-index: 32
(Harvard University),
Shih-Chung Chang8
Estimated H-index: 8
(Harvard University)
+ 3 AuthorsAlfred L. Goldberg133
Estimated H-index: 133
(Harvard University)
Summary The 20S proteasome functions in protein degradation in eukaryotes together with the 19S ATPases or in archaea with the homologous PAN ATPase complex. These ATPases contain a conserved C-terminal hydrophobic-tyrosine-X motif (HbYX). We show that these residues are essential for PAN to associate with the 20S and open its gated channel for substrate entry. Upon ATP binding, these C-terminal residues bind to pockets between the 20S's α subunits. Seven-residue or longer peptides from PAN's C ...
347 Citations Source Cite
Published on Feb 1, 2007in Nature 43.07
Remco Sprangers24
Estimated H-index: 24
(U of T: University of Toronto),
Lewis E. Kay100
Estimated H-index: 100
(U of T: University of Toronto)
The machinery used by the cell to perform essential biological processes is made up of large molecular assemblies. One such complex, the proteasome, is the central molecular machine for removal of damaged and misfolded proteins from the cell. Here we show that for the 670-kilodalton 20S proteasome core particle it is possible to overcome the molecular weight limitations that have traditionally hampered quantitative nuclear magnetic resonance (NMR) spectroscopy studies of such large systems. This...
337 Citations Source Cite
Published on Oct 1, 2005in Nature 43.07
Yuko Hirano11
Estimated H-index: 11
,
Klavs B. Hendil33
Estimated H-index: 33
(UCPH: University of Copenhagen)
+ 6 AuthorsShigeo Murata46
Estimated H-index: 46
(National Presto Industries)
The 26S proteasome is a multisubunit protease responsible for regulated proteolysis in eukaryotic cells1,2. It comprises one catalytic 20S proteasome and two axially positioned 19S regulatory complexes3. The 20S proteasome is composed of 28 subunits arranged in a cylindrical particle as four heteroheptameric rings, α1–7β1–7β1–7α1–7 (refs 4, 5), but the mechanism responsible for the assembly of such a complex structure remains elusive. Here we report two chaperones, designated proteasome assembli...
171 Citations Source Cite
Cited By2
Newest
Published on Dec 14, 2018
Julie A. Maupin-Furlow30
Estimated H-index: 30
(UF: University of Florida)
Archaea are phylogenetically distinct from bacteria, and some of their proteolytic systems reflect this distinction. Here, the current knowledge of archaeal proteolysis is reviewed as it relates to protein metabolism, protein homeostasis, and cellular regulation including targeted proteolysis by proteasomes associated with AAA-ATPase networks and ubiquitin-like modification. Proteases and peptidases that facilitate the recycling of peptides to amino acids as well as membrane-associated and integ...
Source Cite
Published on Dec 14, 2017in Biophysical Reviews
Koichi Kato50
Estimated H-index: 50
(Nagoya City University),
Tadashi Satoh15
Estimated H-index: 15
(Nagoya City University)
Molecular organization in biological systems comprises elaborately programmed processes involving metastable complex formation of biomolecules. This is exemplified by the formation of the proteasome, which is one of the largest and most complicated biological supramolecular complexes. This biomolecular machinery comprises approximately 70 subunits, including structurally homologous, but functionally distinct, ones, thereby exerting versatile proteolytic functions. In eukaryotes, proteasome forma...
3 Citations Source Cite