Positive Cooperativity of the p97 AAA ATPase Is Critical for Essential Functions

被引：38

作者：

Nishikori, Shingo ^{[1
]}

Esaki, Masatoshi ^{[1
]}

Yamanaka, Kunitoshi ^{[1
]}

Sugimoto, Shinya ^{[1
]}

Ogura, Teru ^{[1
]}

机构：

[1] Kumamoto Univ, Inst Mol Embryol & Genet, Dept Mol Cell Biol, Kumamoto 8600811, Japan

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2011年 / 286卷 / 18期

基金：

日本科学技术振兴机构; 日本学术振兴会;

关键词：

ENDOPLASMIC-RETICULUM; CAENORHABDITIS-ELEGANS; MEMBRANE-FUSION; PROTEIN VCP; ER; HYDROLYSIS; P97/VCP; BINDING; CYCLE;

D O I：

10.1074/jbc.M110.201400

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

p97 is composed of two conserved AAA (ATPases associated with diverse cellular activities) domains, which form a tandem hexameric ring. We characterized the ATP hydrolysis mechanism of CDC-48.1, a p97 homolog of Caenorhabditis elegans. The ATPase activity of the N-terminal AAA domain was very low at physiological temperature, whereas the C-terminal AAA domain showed high ATPase activity in a coordinated fashion with positive cooperativity. The cooperativity and coordination are generated by different mechanisms because a noncooperative mutant still showed the coordination. Interestingly, the growth speed of yeast cells strongly related to the positive cooperativity rather than the ATPase activity itself, suggesting that the positive cooperativity is critical for the essential functions of p97.

引用

页码：15815 / 15820

页数：6

共 30 条

[1] Classification of AAA+ proteins [J].

Ammelburg, Moritz ;

Frickey, Tancred ;

Lupas, Andrei N. .

JOURNAL OF STRUCTURAL BIOLOGY, 2006, 156 (01) :2-11

[2] An Intersubunit Signaling Network Coordinates ATP Hydrolysis by m-AAA Proteases [J].

Augustin, Steffen ;

Gerdes, Florian ;

Lee, Sukyeong ;

Tsai, Francis T. F. ;

Langer, Thomas ;

Tatsuta, Takashi .

MOLECULAR CELL, 2009, 35 (05) :574-585

[3] Role of the ubiquitin-selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates [J].

Braun, S ;

Matuschewski, K ;

Rape, M ;

Thoms, S ;

Jentsch, S .

EMBO JOURNAL, 2002, 21 (04) :615-621

[4] Analysis of nucleotide binding to p97 reveals the properties of a tandem AAA hexameric ATPase [J].

Briggs, Louise C. ;

Baldwin, Geoff S. ;

Miyata, Non ;

Kondo, Hisao ;

Zhang, Xiaodong ;

Freemont, Paul S. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (20) :13745-13752

[5] A DIRECT COLORIMETRIC ASSAY FOR CA-2+-STIMULATED ATPASE ACTIVITY [J].

CHAN, KM ;

DELFERT, D ;

JUNGER, KD .

ANALYTICAL BIOCHEMISTRY, 1986, 157 (02) :375-380

[6] Improved structures of full-length p97, an AAA ATPase: Implications for mechanisms of nucleotide-dependent conformational change [J].

Davies, Jason M. ;

Brunger, Axel T. ;

Weis, William I. .

STRUCTURE, 2008, 16 (05) :715-726

[7] Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-ray scattering [J].

Davies, JM ;

Tsuruta, H ;

May, AP ;

Weis, WI .

STRUCTURE, 2005, 13 (02) :183-195

[8] Nucleotide dependent motion and mechanism of action of p97/VCP [J].

DeLaBarre, B ;

Brunger, AT .

JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (02) :437-452

[9] Central pore residues mediate the p97/VCP activity required for ERAD [J].

DeLaBarre, Byron ;

Christianson, John C. ;

Kopito, Ron R. ;

Brunger, Axel T. .

MOLECULAR CELL, 2006, 22 (04) :451-462

[10]

Esaki M, 2010, BIOCHEM CELL BIOL, V88, P109, DOI [10.1139/O09-116, 10.1139/o09-116]

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