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Identification of a haem domain in human soluble adenylate cyclase.

Title data

Middelhaufe, Sabine ; Leipelt, Martina ; Levin, Lonny R. ; Buck, Jochen ; Steegborn, Clemens:
Identification of a haem domain in human soluble adenylate cyclase.
In: Bioscience Reports. Vol. 32 (October 2012) Issue 5 . - pp. 491-499.
ISSN 0144-8463
DOI: https://doi.org/10.1042/BSR20120051

Project information

Project financing: Europäische Strukturfonds

Abstract in another language

The second messengers cAMP and cGMP mediate a multitude of physiological processes. In mammals, these cyclic nucleotides are formed by related Class III nucleotidyl cyclases, and both ACs (adenylate cyclases) and GCs (guanylate cyclases) comprise transmembrane receptors as well as soluble isoforms. Whereas sGC (soluble GC) has a well-characterized regulatory HD (haem domain) that acts as a receptor for the activator NO (nitric oxide), very little is known about the regulatory domains of the ubiquitous signalling enzyme sAC (soluble AC). In the present study, we identify a unique type of HD as a regulatory domain in sAC. The sAC-HD (sAC haem domain) forms a larger oligomer and binds, non-covalently, one haem cofactor per monomer. Spectral analyses and mutagenesis reveal a 6-fold co-ordinated haem iron atom, probably with non-typical axial ligands, which can bind both NO and CO (carbon monoxide). Splice variants of sAC comprising this domain are expressed in testis and skeletal muscle, and the HD displays an activating effect on the sAC catalytic core. Our results reveal a novel mechanism for regulation of cAMP signalling and suggest a need for reanalysis of previous studies on mechanisms of haem ligand effects on cyclic nucleotide signalling, particularly in testis and skeletal muscle.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 14512417
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 17 Apr 2015 09:51
Last Modified: 17 Apr 2015 09:51
URI: https://eref.uni-bayreuth.de/id/eprint/10384