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Titolo:
Physical characterization of plakophilin 1 reconstituted with and without zinc
Autore:
Hofmann, I; Mucke, N; Reed, J; Herrmann, H; Langowski, J;
Indirizzi:
German Canc Res Ctr, Div Cell Biol, D-69120 Heidelberg, Germany German Canc Res Ctr Heidelberg Germany D-69120 69120 Heidelberg, Germany German Canc Res Ctr, Div Biophys Macromol, D-69120 Heidelberg, Germany German Canc Res Ctr Heidelberg Germany D-69120 69120 Heidelberg, Germany German Canc Res Ctr, Div Pathochem, D-69120 Heidelberg, Germany German Canc Res Ctr Heidelberg Germany D-69120 69120 Heidelberg, Germany
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 14, volume: 267, anno: 2000,
pagine: 4381 - 4389
SICI:
0014-2956(200007)267:14<4381:PCOP1R>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DESMOSOMAL PLAQUE PROTEIN; PARENTERAL-NUTRITION; HUMAN PLAKOGLOBIN; CRYSTAL-STRUCTURE; BAND-6 PROTEIN; FAMILY; METALLOTHIONEIN; SEQUENCE; BINDING; DIFFERENTIATION;
Keywords:
arm-repeat protein; zinc-binding domains; analytical ultracentrifugation; circular dichroism; dynamic light scattering;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Hofmann, I German Canc Res Ctr, Div Cell Biol, Neuenheimer Feld 280, D-69120 Heidelberg, Germany German Canc Res Ctr Neuenheimer Feld 280 HeidelbergGermany D-69120
Citazione:
I. Hofmann et al., "Physical characterization of plakophilin 1 reconstituted with and without zinc", EUR J BIOCH, 267(14), 2000, pp. 4381-4389

Abstract

Plakophilin 1 (PKP1) belongs to the arm-repeat protein family which is characterized by the presence of a conserved 42-amino-acid motif. Despite individual members of the family containing a similar type of structural domain, they exhibit diverse cellular functions. PKP1 is ubiquitously expressed in human tissues and, depending on the type of cell, found prominently in the karyoplasm and/or in desmosomes. In surface plasmon resonance detection experiments, we noticed that PKP1 specifically bound zinc but not calcium ormagnesium. Therefore we have used circular dichroism spectroscopy, limitedproteolysis, analytical ultracentrifugation, electron microscopy and dynamic light scattering to establish the physical properties of recombinant PKP1 depending on the presence or absence of zinc. The alpha helix content of PKP1 was considerably higher when reconstituted with zinc than without. By atomic absorption spectroscopy 7.3 atoms zinc were shown to be tightly associated with one molecule of wild-type PKP1. The zinc-reconstituted protein formed globular particles of 21.9 +/- 8.4 nm diameter, as measured by electron microscopy after glycerol spraying/rotary metal shadowing. In parallel,the average sedimentation coefficient (s(20,w)) for zinc-containing PKP1 was 41S and its diffusion coefficient, as obtained by dynamic light scattering, 1.48 x 10(-7) cm(2).s(-1). The molecular mass of 2.44 x 10(6) obtained from s and D yields an average stoichiometry of 30 for the PKP1 oligomer. In contrast, PKP1, reconstituted without zinc, contained no significant amount of zinc, sedimented with 4.6S, and was present in monomeric form as determined by sedimentation equilibrium centrifugation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/08/20 alle ore 19:57:35