Evolution and Phylogenetics in the Globin Superfamily. From Sequence to Structure to Function.

SCHUSTER, CLAUDIO DAVID; BUSTAMANTE, JUAN PABLO; MARTÍ, MARCELO ADRIÁN

Mar del Plata

Congreso; 9CAB2C (IX Congreso Argentino de Bioinformática y Biología Computacional); 2018

Asoaciación Argentina de Bioinformática y Biología Computacional

Globins constitute a protein superfamily whose typical representatives are mammalian myoglobin and hemoglobin. They are ubiquitous, covering the whole spectrum of biological diversity and are found in almost all living forms, both eukaryotes and prokaryotes. Their characteristic structure consists of two pairs (or trios) of alpha helices folded one over the other like a sandwich, inside which lies a heme group that comprises the active site. It is the heme iron that through interactions with smaller molecules like O2, NO or CO, allows them to perform their function, commonly associated with reactivity, transport and detection of those small biomolecules. Several sequence and phylogenetic analysis of globins have been carried out in the last twenty years. Nonetheless, these studies have always been limited to specific taxonomic groups (bacteria, algae, vertebrates, etc), or to specific globin subfamilies (Bac Globin, Protoglobin or Globin). Moreover, considering that protein databases such as Uniprot have grown spectacularly in recent years due to the NGS projects, it becomes necessary to perform an update on the newly found globin sequences and a phylogenetic analysis comprising all their diversity in every domain of life. To fulfill this task, in the present work we performed first datamining over the three known globin families, collecting around 30 thousand sequences. We defined using HMM each family?s profile and some inner groups? profiles. In the future we intend to carry out a phylogenetic analysis by bayesian inference for each individual family of these proteins and another one of the whole superfamily. We also intend to carry out other analysis of biological interest such as searching for secondary structure in the N and C terminal ends, and to study the most common types of domain associated with globins when these last ones are polimeric.