Ca2plus differently affects hydrophobic properties of guanylyl cyclase-activating proteins [GCAPs] and recoverin

• Autorzy: Gorczyca W. A. , Kobialka M. , Kuropatwa M. , Kurowska E.
• Języki publikacji: EN

Abstrakty

EN

Guanylyl cyclase-activating proteins (GCAPs) and recoverin are retina-specific Ca2+ -binding proteins involved in phototransduction. We provide here evidence that in spite of structural similarities GCAPs and recoverin differently change their overall hydrophobic properties in response to Ca2+ . Using native bovine GCAP1, GCAP2 and recoverin we show that: i) the Ca2+ -dependent binding of recoverin to Phenyl-Se- pharose is distinct from such interactions of GCAPs; ii) fluorescence intensity of 1-anilinonaphthalene-8-sulfonate (ANS) is markedly higher at high [Ca2+ ]free (10 uM) than at low [Ca2+ ]freee(10 nM) in the presence of recoverin, while an opposing effect is observed in the presence of GCAPs; iii) fluorescence resonance energy transfer from tryptophane residues to ANS is more efficient at high [Ca2+ ]free in recoverin and at low [Ca2+ ]freee in GCAP2. Such different changes of hydrophobicity evoked by Ca2+ ap­pear to be the precondition for possible mechanisms by which GCAPs and recoverin control the activities of their target enzymes.

Słowa kluczowe

EN

neuronal calcium sensor; recoverin; guanylyl cyclase; calcium binding protein; fluorescence; monoclonal antibody; guanylyl cyclase-activating protein; phototransduction; hydrophobic property

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 2
• Opis fizyczny: p.367-376,fig.

Twórcy

autor

Gorczyca W. A.

• Polish Academy of Sciences, R.Weigla 12, 53-114 Wroclaw, Poland

autor

Kobialka M.

autor

Kuropatwa M.

autor

Kurowska E.

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