Solution structure and dynamics of glia maturation factor from Caenorhabditis elegans |
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| Institution: | 1. Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow 226031, India;2. Academy of Scientific and Innovative Research, New Delhi 110025, India;3. Centre of Biomedical Research (CBMR), Sanjay Gandhi Post-Graduate Institute of Medical Sciences, Raibareli Road, Lucknow, Uttar Pradesh 226014, India;1. IRCCS SDN, 80143 Napoli, Italy;2. Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy;3. Institute of Food Science, CNR, Via Roma, 64 Avellino, Italy;1. Department of Biochemistry and Cell Biology, Faculty of Natural Sciences, Kazimierz Wielki University in Bydgoszcz, Ks. J. Poniatowskiego 12 Str., 85-671 Bydgoszcz, Poland;2. Department of Physics, University at Buffalo, SUNY, Buffalo, NY 14260, United States;1. Faculty of Pharmacy, Meijo University, 150 Yagotoyama, Tempaku-ku, Nagoya, Aichi 468-8503, Japan;2. Institute of Medical, Pharmaceutical and Health Sciences, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan;3. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan;4. Faculty of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japan;1. Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India;2. CSIR, Central Drug Research Institute, Lucknow 226031, India;3. King Saud University, Riyadh, Saudi Arabia |
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| Abstract: | BackgroundThe 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 GMFγ of human and mouse and is 138 amino acids in length.MethodsWe have characterized the solution structure and dynamics of CeGMF by solution NMR spectroscopy and its thermal stability by DSC.ResultsThe solution structure of CeGMF shows canonical ADF-H fold with two additional β-strands in the β4-β5 loop region. The Site-1 of CeGMF is well formed and residues of all three regions of Site-1 show dynamic flexibility. However, the β4-β5 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 β4-β5 loop is low in comparison to corresponding F-loop region of ADF/cofilin UNC-60B. A general difference in packing of α3 and α1 between GMF and ADF/cofilins was noticed. Additionally, thermal stability of CeGMF was significantly higher than its ADF/cofilin homologs.ConclusionWe 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 significanceThis study provides a useful insight to structural and dynamics factors that define the specificity of GMF towards Arp2/3 complex. |
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