GTP-binding properties of the membrane-bound form of porcine liver annexin VI

• Autorzy: Kirilenko A. , Golczak M. , Pikula S. , Bandorowicz-Pikula J.
• Języki publikacji: EN

Abstrakty

EN

Annexin VI (AnxVI) of molecular mass 68-70 kDa belongs to a multigenic family of ubiquitous Ca2+ - and phospholipid-binding proteins. In this report, we describe the GTP-binding properties of porcine liver AnxVI, determined with a fluorescent GTP analogue, 2-(or 3')-0-(2,4,6-trinitrophenyl)guanosine 5' -triphosphate (TNP-GTP). The optimal binding of TNP-GTP to AnxVI was observed in the presence of Ca2+ and asolectin liposomes, as evidenced by a 5.5-fold increase of TNP-GTP fluorescence and a concomitant blue shift (by 17 nm) of its maximal emission wavelength. Titration of AnxVI with TNP-GTP resulted in the determination of the dissociation constant (Kd) and binding stoichiometry that amounted to 1.3 uM and 1:1 TNP-GTP/AnxVI, mole/mole, respectively. In addition, the intrinsic fluorescence of the membrane- bound form of AnxVI was quenched by TNP-GTP and this was accompanied by fluo­rescence resonance energy transfer (FRET) from AnxVI Trp residues to TNP-GTP. This indicates that the GTP-binding site within the AnxVI molecule is probably located in the vicinity of a Trp-containing domain of the protein. By controlled proteolysis of human recombinant AnxVI, followed by purification of the proteolytic fragments by affinity chromatography on GTP-agarose, we isolated a 35 kDa fragment correspond­ing to the N-terminal half of AnxVI containing Trp192 . On the basis of these results, we suggest that AnxVI is a GTP-binding protein and the binding of the nucleotide may have a regulatory impact on the interaction of annexin with membranes, e.g. forma­tion of ion channels by the protein.

Słowa kluczowe

EN

fluorescence resonance energy transfer; epidermal growth factor; liposome; porcine liver; calcium; molecular mass; circular dichroism; liver; annexin VI; phospholipid

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2001
• Tom: 48
• Numer: 4
• Opis fizyczny: p.851-865,fig.

Twórcy

autor

Kirilenko A.

• M.Nencki Institute of Experimental Biology, L.Pasteura 3, 02-093 Warsaw, Poland

autor

Golczak M.

autor

Pikula S.

autor

Bandorowicz-Pikula J.

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