Role of External Loops of Human Ceruloplasmin in Copper Loading by ATP7B and Ccc2p

被引:12
作者
Maio, Nunziata
Polticelli, Fabio
De Francesco, Giovanni [1 ]
Rizzo, Gianluca
di Patti, Maria Carmela Bonaccorsi [1 ]
Musci, Giovanni [2 ,3 ]
机构
[1] Univ Roma La Sapienza, Dept Sci Biochim, I-00185 Rome, Italy
[2] Univ ROMA TRE, Dipartimento Biol, I-00146 Rome, Italy
[3] Univ Molise, Dipartimento Sci & Tecnol Agroalimentari, I-86100 Campobasso, Italy
关键词
PICHIA-PASTORIS; ACERULOPLASMINEMIA; EXPRESSION; DISORDER; ATPASES; PROTEIN; SYSTEM;
D O I
10.1074/jbc.M109.090027
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
Ceruloplasmin is a multicopper oxidase required for correct iron homeostasis. Previously, we have identified a ceruloplasmin mutant associated with the iron overload disease aceruloplasminemia, which was unable to acquire copper from themammalian pump ATP7B but could be produced in an enzymatically active form in yeast. Here, we report the expression of recombinant ceruloplasmin in the yeast Pichia pastoris and the study of the role of five surface-exposed loops in copper incorporation by comparing the efficiencies of mammalian ATP7B and yeast Ccc2p. The possibility to "mix and match" mammalian and yeast multicopper oxidases and copper ATPases can provide clues on the molecular features underlying the process of copper loading in multicopper oxidases.
引用
收藏
页码:20507 / 20513
页数:7
相关论文
共 18 条
[1]   Site-directed mutagenesis of human ceruloplasmin - Production of a proteolytically stable protein and structure-activity relationships of type 1 sites [J].
Bielli, P ;
Bellenchi, GC ;
Calabrese, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (04) :2678-2685
[2]   Dominant Mutants of Ceruloplasmin Impair the Copper Loading Machinery in Aceruloplasminemia [J].
Bonaccorsi di Patti, Maria Carmela ;
Maio, Nunziata ;
Rizzo, Gianluca ;
De Francesco, Giovanni ;
Persichini, Tiziana ;
Colasanti, Marco ;
Polticelli, Fabio ;
Musci, Giovanni .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (07) :4545-4554
[3]   New selectable marker/auxotrophic host strain combinations for molecular genetic manipulation of Pichia pastoris [J].
Cereghino, GPL ;
Cereghino, JL ;
Sunga, AJ ;
Johnson, MA ;
Lim, M ;
Gleeson, MAG ;
Cregg, JM .
GENE, 2001, 263 (1-2) :159-169
[4]   Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin [J].
De Domenico, Ivana ;
Ward, Diane McVey ;
Di Patti, Maria Carmela Bonaccorsi ;
Jeong, Suh Young ;
David, Samuel ;
Musci, Giovanni ;
Kaplan, Jerry .
EMBO JOURNAL, 2007, 26 (12) :2823-2831
[5]   Release of highly active Fet3 from membranes of the yeast Pichia pastoris by limited proteolysis [J].
di Patti, MCB ;
Bellenchi, GC ;
Bielli, P ;
Calabrese, L .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 372 (02) :295-299
[6]   Sequence variation in the ATP-binding domain of the Wilson disease transporter, ATP7B, affects copper transport in a yeast model system [J].
Hsi, Gloria ;
Cullen, Lara A. ;
Macintyre, Georgina ;
Chen, Matthew M. ;
Glerum, D. Moira ;
Cox, Diane W. .
HUMAN MUTATION, 2008, 29 (04) :491-501
[7]   Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae [J].
Hung, IH ;
Suzuki, M ;
Yamaguchi, Y ;
Yuan, DS ;
Klausner, RD ;
Gitlin, JD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (34) :21461-21466
[8]   Extrapyramidal and cerebellar movement disorder in association with heterozygous ceruloplasmin gene mutation [J].
Kuhn, J ;
Miyajima, H ;
Takahashi, Y ;
Kunath, B ;
Hartmann-Klosterkoetter, U ;
Cooper-Mahkorn, D ;
Schaefer, M ;
Bewermeyer, H .
JOURNAL OF NEUROLOGY, 2005, 252 (01) :111-113
[9]   Cellular multitasking: The dual role of human Cu-ATPases in cofactor delivery and intracellular copper balance [J].
Lutsenko, Svetlana ;
Gupta, Arnab ;
Burkhead, Jason L. ;
Zuzel, Vesna .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2008, 476 (01) :22-32
[10]   Function and regulation of human copper-transporting ATPases [J].
Lutsenko, Svetlana ;
Barnes, Natalie L. ;
Bartee, Mee Y. ;
Dmitriev, Oleg Y. .
PHYSIOLOGICAL REVIEWS, 2007, 87 (03) :1011-1046