Authors:

Alex Cain

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About Paper:

Fic (Filamentation induced by cAMP)-domain-containing proteins are an emerging family of enzymes known to carry out post-translational modifications (PTMs) via the addition of phosphate-containing groups, such as AMP, onto alcohol-containing amino acids of their target proteins. Fic-domain-containing proteins occur in a wide range of organisms, but many occur in bacteria, where they often function as a means of pathogenesis. We have discovered a highly conserved Fic-domain-containing protein in Bordetella bronchiseptica, a small gram-negative bacteria which sometimes infects household pets. Discovering more about the structure and binding targets of this protein (BbFic) may reveal important information about other Bordetella Fic-domain- containing proteins, such as that of Bordetella pertussis, which is responsible for whooping cough. BbFic has been found to carry out a previously unseen PTM, GMPylation, but the targets remain unclear. We solved the crystal structure of apo BbFic at 3.1 Å and using AlphaFold predicted a putative function of BbFic. This analysis predicts that the C-terminus of BbFic has a helix-turn-helix motif and translocates to the nucleus in mammalian cells, leading us to hypothesize that BbFic may be involved in DNA binding. Our experiments aim to express and purify the C-terminus of BbFic. Once the protein has been sufficiently purified, it will be used in X-ray crystallography and pulldown assays to determine its structure and binding targets, respectively.

Source:

Purdue University / 2023

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Co-authors:

Alex Cain