Abstract:
:To study the fluctuations of cGMP in living cells through changes of energy transfer of dissociable fluorescence labeled subunits, we constructed a cGMP-sensitive probe by combining the N-terminus of the type I regulatory subunit of cAMP-dependent protein kinase (PKA) with the cGMP binding sites of cGMP-dependent protein kinase I alpha (PKG). This chimeric regulatory subunit retained PKA-like dimerization and PKG-compatible cGMP binding constants (Kd = 53 nM) for both binding sites. High affinity interaction with the PKA catalytic subunit was verified by Surface Plasmon Resonance (Kd = 3.15 nM). Additionally, the chimera inhibits the formation of wild-type holoenzyme with an apparent Ki of 1.05 nM. Furthermore, cGMP dissociated the mutant holoenzyme with an apparent activation constant of 146 nM. Thus, our construct provides all the requirements needed to investigate changes in intracellular cGMP concentrations.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Wild N,Herberg FW,Hofmann F,Dostmann WRdoi
10.1016/0014-5793(95)01146-6subject
Has Abstractpub_date
1995-11-06 00:00:00pages
356-62issue
3eissn
0014-5793issn
1873-3468pii
0014579395011466journal_volume
374pub_type
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