Lessons from the post-genomic era: Globin diversity beyond oxygen binding and transport

Redox Biology

Serge N. Vinogradov¹  Ilaria M.C. Orlando²  David Hoogewijs²  Darko Maric²  Teng Wei Koay²  Miguel Correia²  Anna Keppner² 

[1] Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, USA;Section of Medicine, Department of Endocrinology, Metabolism and Cardiovascular System, University of Fribourg, Fribourg, Switzerland;

关键词: Cancer;    Hemoglobin;    Hypoxia;    Myoglobin;    Nitric oxide;    Oxidative stress;   

DOI  :  

来源: DOAJ

【 摘 要 】

Vertebrate hemoglobin (Hb) and myoglobin (Mb) were among the first proteins whose structures and sequences were determined over 50 years ago. In the subsequent pregenomic period, numerous related proteins came to light in plants, invertebrates and bacteria, that shared the myoglobin fold, a signature sequence motif characteristic of a 3-on-3 α-helical sandwich. Concomitantly, eukaryote and bacterial globins with a truncated 2-on-2 α-helical fold were discovered. Genomic information over the last 20 years has dramatically expanded the list of known globins, demonstrating their existence in a limited number of archaeal genomes, a majority of bacterial genomes and an overwhelming majority of eukaryote genomes. In vertebrates, 6 additional globin types were identified, namely neuroglobin (Ngb), cytoglobin (Cygb), globin E (GbE), globin X (GbX), globin Y (GbY) and androglobin (Adgb). Furthermore, functions beyond the familiar oxygen transport and storage have been discovered within the vertebrate globin family, including NO metabolism, peroxidase activity, scavenging of free radicals, and signaling functions. The extension of the knowledge on globin functions suggests that the original roles of bacterial globins must have been enzymatic, involved in defense against NO toxicity, and perhaps also as sensors of O2, regulating taxis away or towards high O2 concentrations. In this review, we aimed to discuss the evolution and remarkable functional diversity of vertebrate globins with particular focus on the variety of non-canonical expression sites of mammalian globins and their according impressive variability of atypical functions.

【 授权许可】

Unknown