Prediction of mutations on structure primase of the archaeon Sulfolobus solfataricus

• Published in: Acta scientiarum. Biological sciences Vol. 39; no. 4; p. 463
• Main Authors: Souza, Eden Silva e, Diniz, Michely Correia
• Format: Journal Article
• Language: English
• Published: Maringa Editora da Universidade Estadual de Maringá - EDUEM 24.11.2017; Universidade Estadual de Maringá
• Subjects: 3D structure; Aspartic acid; Bioinformatics; DNA biosynthesis; DNA primase; DNA replication; Eukaryotes; Free energy; Glutamic acid; in silico; Mutation; mutations; PriL; Primase; primer; Primers; Replication; Ribonucleic acid; RNA
• ISSN: 1679-9283; 1807-863X
• DOI: 10.4025/actascibiolsci.v39i4.34600

All living organisms need a DNA replication mechanism and it has been conserved in the three domains of life throughout evolutionary process. Primase is the enzyme responsible for synthesizing de novo RNA primers in DNA replication. Archaeo-Eukaryotic Primase (AEP) is the superfamily that typically forms a heterodimeric complex containing both a small catalytic subunit (PriS) and a large accessory noncatalytic subunit (PriL). Sulfolobus solfataricus is a model organism for research on the Genetics field. The aim of this work was to evaluate, via Bioinformatics tools, three mutations in the large subunit (PriL) of the archaeon Sulfolobus solfataricus. The aspartic acid residue in the positions (Asp) 62, (Asp) 235, (Asp) 241 have been substituted by glutamic acid (Glu). The highest positive free energy variation of the three substitutions analyzed occurred with the mutation at the (Asp) 241 site. The in silico analysis suggested that these mutations in PriL may destabilize its tridimensional structure interfering with replication mechanisms of Sulfolobus solfataricus. Moreover, it may also alter interactions with other molecules, making salt bridges, for instance.