Fig. 1 | Scientific Reports

Fig. 1

From: Differential GTP-dependent in-vitro polymerization of recombinant Physcomitrella FtsZ proteins

Fig. 1

FtsZ domain structures, sequence identity and analysis of the co-immunoprecipitations (Co-IPs) against GFP-tagged FtsZ2-1 protein. (A) Domain structures of the five Physcomitrella FtsZ proteins and the FtsZ2-1_GFP fusion protein. Depicted are PFAM67 domains (FtsZ family, C-terminal domain: PF12327; Tubulin/FtsZ family, GTPase domain: PF00091; GFP: PF01353) and the poly-G linker in the FtsZ2-1_GFP fusion protein. Arrows indicate predicted chloroplast transit peptide (cTP) cleavage sites (blue: ChloroP1.1; green: TargetP2.0). Predicted cTP cleavage sites of other FtsZ isoforms than FtsZ1-2 and FtsZ2-1 are not shown. The image was created with the R package drawProteins68. (B) The volcano plot shows the log2 ratios of normalized LFQ (label-free quantitation) intensities plotted against log10 of adjusted p-values. Proteins significantly enriched in the GFP-tagged pulldown are shown as red crosses with a false discovery rate (FDR) of 0.01%. Physcomitrella wild type (WT) served as a negative control. Proteins not significant for neither WT nor FtsZ2-1_GFP are visualized as grey crosses. The Co-IP was performed with GFP-Trap Magnetic Particles M-270 (ChromoTek GmbH, Planegg, Germany) and Physcomitrella protonema tissue homogenized from suspension culture. The isoforms of FtsZ1 (FtsZ1-1, FtsZ1-2) could not be distinguished on the basis of the peptides identified in this approach and are thus grouped (FtsZ1). (C) Matrix showing the sequence identity ([%]) between the five different FtsZ isoforms. Identity values were obtained from a multiple sequence alignment using protein sequences done with the UniProt Align tool (https://www.uniprot.org/align).

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