5ynr

Publication Abstract from PubMed

BACKGROUND: The GMF class of the ADF-H domain family proteins regulate actin dynamics by binding to the Arp2/3 complex and F-actin through their Site-1 and Site-2, respectively. CeGMF of C. elegans is analogous to GMFgamma of human and mouse and is 138 amino acids in length. METHODS: We have characterized the solution structure and dynamics of CeGMF by solution NMR spectroscopy and its thermal stability by DSC. RESULTS: The solution structure of CeGMF shows canonical ADF-H fold with two additional beta-strands in the beta4-beta5 loop region. The Site-1 of CeGMF is well formed and residues of all three regions of Site-1 show dynamic flexibility. However, the beta4-beta5 loop of Site-2 is less inclined towards the C-terminal, as the latter is truncated by four residues in comparison to GMF isoforms of human and mouse. Regions of Site-2 show motions on ns-ps timescale, but dynamic flexibility of beta4-beta5 loop is low in comparison to corresponding F-loop region of ADF/cofilin UNC-60B. A general difference in packing of alpha3 and alpha1 between GMF and ADF/cofilins was noticed. Additionally, thermal stability of CeGMF was significantly higher than its ADF/cofilin homologs. CONCLUSION: We have presented the first solution structure of GMF from C. elegans, which highlights the structural differences between the Site-2 of CeGMF and mammalian GMF isoforms. Further, we have seen the differences in structure, dynamics, and thermal stability of GMF and ADF/cofilin. GENERAL SIGNIFICANCE: This study provides a useful insight to structural and dynamics factors that define the specificity of GMF towards Arp2/3 complex.

Solution structure and dynamics of glia maturation factor from Caenorhabditis elegans.,Maheshwari D, Shukla VK, Jain A, Tripathi S, Kumar D, Arora A Biochim Biophys Acta Proteins Proteom. 2018 Jul 6;1866(10):1008-1020. doi:, 10.1016/j.bbapap.2018.06.007. PMID:29981887^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.