RG Biophysical Analysis (BA)
http://hdl.handle.net/10033/6835
AG Biophysikalische Analytik (BA)2024-03-28T12:56:25ZSolution structure of the Equine Infectious Anemia Virus p9 protein: a rationalization of its different ALIX binding requirements compared to the analogous HIV-p6 protein
http://hdl.handle.net/10033/620696
Solution structure of the Equine Infectious Anemia Virus p9 protein: a rationalization of its different ALIX binding requirements compared to the analogous HIV-p6 protein
Sharma, Alok; Bruns, Karsten; Röder, René; Henklein, Peter; Votteler, Jörg; Wray, Victor; Schubert, Ulrich
Abstract Background The equine infection anemia virus (EIAV) p9 Gag protein contains the late (L-) domain required for efficient virus release of nascent virions from the cell membrane of infected cell. Results In the present study the p9 protein and N- and C-terminal fragments (residues 1-21 and 22-51, respectively) were chemically synthesized and used for structural analyses. Circular dichroism and 1H-NMR spectroscopy provide the first molecular insight into the secondary structure and folding of this 51-amino acid protein under different solution conditions. Qualitative 1H-chemical shift and NOE data indicate that in a pure aqueous environment p9 favors an unstructured state. In its most structured state under hydrophobic conditions, p9 adopts a stable helical structure within the C-terminus. Quantitative NOE data further revealed that this α-helix extends from Ser-27 to Ser-48, while the N-terminal residues remain unstructured. The structural elements identified for p9 differ substantially from that of the functional homologous HIV-1 p6 protein. Conclusions These structural differences are discussed in the context of the different types of L-domains regulating distinct cellular pathways in virus budding. EIAV p9 mediates virus release by recruiting the ALG2-interacting protein X (ALIX) via the YPDL-motif to the site of virus budding, the counterpart of the YPXnL-motif found in p6. However, p6 contains an additional PTAP L-domain that promotes HIV-1 release by binding to the tumor susceptibility gene 101 (Tsg101). The notion that structures found in p9 differ form that of p6 further support the idea that different mechanisms regulate binding of ALIX to primary versus secondary L-domains types.
2009-12-17T00:00:00ZFormation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda.
http://hdl.handle.net/10033/561226
Formation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda.
Stoppok, W; Rapp, P; Wagner, F
The formation and location of endo-1,4-beta-glucanases and beta-glucosidases were studied in cultures of Cellulomonas uda grown on microcrystalline cellulose, carboxymethyl cellulose, printed newspaper, and some mono- or disaccharides. Endo-1,4-Glucanases were found to be extracellular, but a very small amount of cell-bound endo-1,4-beta-glucanase was considered to be the basal endoglucanase level of the cells. The formation of extracellular endo-1,4-beta-glucanases was induced by cellobiose and repressed by glucose. Extracellular endoglucanase activity was inhibited by cellobiose but not by glucose. beta-Glucosidases, on the other hand, were formed constitutively and found to be cell bound. beta-Glucosidase activity was inhibited noncompetitively by glucose. Some characteristics such as the optimal pH for and the thermostability of the endoglucanases and beta-glucosidases and the end products of cellulose degradation were determined.
1982-07-01T00:00:00ZInduced production of depsipeptides by co-culturing Fusarium tricinctum and Fusarium begoniae
http://hdl.handle.net/10033/302590
Induced production of depsipeptides by co-culturing Fusarium tricinctum and Fusarium begoniae
Wang, Jian-ping; Lin, Wenhan; Wray, Victor; Lai, Daowan; Proksch, Peter
2013-10-01T00:00:00ZCallyaerin G, a new cytotoxic cyclic peptide from the marine sponge Callyspongia aerizusa
http://hdl.handle.net/10033/293855
Callyaerin G, a new cytotoxic cyclic peptide from the marine sponge Callyspongia aerizusa
Ibrahim, Sabrin R. M.; Edrada-Ebel, RuAngelie; Mohamed,Gamal A.; Youssef, Diaa T. A; Wray, Victor; Proksch, Peter
2008-04-16T00:00:00Z