Spo0M: structure and function beyond regulation of sporulation
In this mini-review, we present a perspective on the recent findings relating Spo0M structure and function that will stimulate and guide further studies in the characterization of this interesting protein. Cell division and sporulation constitute two of the best studied processes in the model organism Bacillus subtilis; however, there are many missing pieces in the giant regulatory puzzle that governs the independent and shared networks between them. Spo0M is a little studied protein that has been related to both, cell division and sporulation, but its biochemical function and its direct interactions have not been yet defined. Structural analysis of Spo0M revealed the presence of an arrestin-like domain and an FP domain (a dimerization domain present in proteasome elements), motifs more commonly found in eukaryotic proteins. The aim of this perspective is to present open questions regarding the functional and structural features of Spo0M that make this protein a good candidate for the ancestor of arrestins in bacteria and an important element in developmental and differentiation processes of Bacillus subtilis.
KeywordsSpo0M Bacillus subtilis Sporulation Cell division Arrestins Stress response
We thank Dr. Enrique Merino and Dr. Rosa María Gutiérrez-Ríos for enriching discussions regarding the genetic context, homology, and physiology of Spo0M. We thank Shirley Ainsworth for bibliographical assistance. This work was supported partially by CONACyT 176381 and DGAPA IN 204016. Luz Adriana Vega-Cabrera was supported by a CONACyT and DGAPA scholarship.
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest.
- Aubry L, Klein G (2013) True arrestins and arrestin-fold proteins: a structure-based appraisal. In: Khalil RA (ed) Progress in molecular biology and translational science, vol 118. Elsevier Inc, London, UK, pp 21–56Google Scholar
- Driks A, Eichenberger P (2016) The spore coat. Microbiol Spectr 4(2). doi: 10.1128/microbiolspec.TBS-0023-2016
- Gurevich VV, Gurevich EV (2013) Structural determinants of arrestin function. In: Khalil RA (ed) Progress in molecular biology and translational science, vol 118. Elsevier Inc, London, UK, pp 57–92Google Scholar
- Jeleń F, Oleksy A, Śmietana K (2003) PDZ domains—common players in the cell signaling. Acta Biochim Pol 50(4):985–1017Google Scholar
- Lefkowitz RJ (2013) Arrestins come of age: a personal historical perspective. In: Khalil RA (ed) Progress in molecular biology and translational science, vol 118. Elsevier Inc, London, UK, pp 3–18Google Scholar