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A Universal Stress Protein (USP) in Mycobacteria binds cAMP

Titelangaben

Banerjee, Arka ; Adolph, Ramona S. ; Gopalakrishnapai, Jayashree ; Kleinbölting, Silke ; Emmerich, Christiane ; Steegborn, Clemens ; Visweswariah, Sandhya S.:
A Universal Stress Protein (USP) in Mycobacteria binds cAMP.
In: The Journal of Biological Chemistry. Bd. 290 (2015) Heft 20 . - S. 12731-12743.
ISSN 1083-351X
DOI: https://doi.org/10.1074/jbc.M115.644856

Abstract

Mycobacteria are endowed with rich and diverse machinery for the synthesis, utilization and degradation of cAMP. The actions of cyclic nucleotides are generally mediated by binding of cAMP to conserved and well-characterized cyclic nucleotide binding (CNB) domains, or structurally distinct GAF domain-containing proteins. Proteins with CNB and GAF domains can be identified in the genome of Mycobacterial species and some of them have been characterized. Here we show that a significant fraction of intracellular cAMP is bound to protein in Mycobacterial species, and using affinity chromatography techniques, identify specific universal stress proteins (USP) as abundantly expressed cAMP-binding proteins in slow-growing as well as fast growing Mycobacteria. We have characterized the biochemical and thermodynamic parameters for binding of cAMP, and show that these USPs bind cAMP with a higher affinity than ATP, an established ligand for other USPs. We determined the structure of the USP MSMEG_3811 bound to cAMP and confirmed through structure guided mutagenesis residues important for cAMP binding. This family of USPs is conserved in all Mycobacteria and we suggest that they serve as 'sinks' for cAMP, making this second messenger available for downstream effectors as and when ATP levels are altered in the cell.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie > Lehrstuhl Biochemie I - Proteinbiochemie der Signaltransduktion - Univ.-Prof. Dr. Clemens Steegborn
Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 540 Chemie
Eingestellt am: 20 Apr 2015 15:19
Letzte Änderung: 16 Jun 2023 07:36
URI: https://eref.uni-bayreuth.de/id/eprint/10438