Assembly Domain

Igarashi, K., Fujita, N., and Ishihama, A. (1991). Identification ofa subunit assembly domain in the alpha subunit ofEscherichia coli RNA polymerase. J. Mol. Biol. 218, 1-6. 

Smith MJ, Beck M, Stephenson FA. 2003. Can the yeast two-hybrid system be used to study assembly domains of GABA-A receptor subunits British Neurosci Assoc Abstr 17 26.12. 

There are at least two assembly domains, namely the L20 domain and the L15 domain, in the 50 S assembly map (Fig. 15). Proteins within the L20 domain are essential for the assembly but not for the function of the 50 S subunit whereas those in the L15 domain are functionally important proteins whose assembly occurs at a late state. As with the 30 S subunit, the assembly map of the 50 S subunit (Rohl and Nierhaus, 1982) not only reflects the assembly dependence but also the topographical relationship of the proteins within the ribosomal particle. This conclusion is supported by a good correspondence between the assembly map on the one hand, and results from cross-linking studies and from the sequential removal of proteins from the particle by LiCl on the other hand. There is also a correlation between the interdependence of proteins during the assembly process and the arrangement of their genes on the E. coli chromosome (Rbhl et al., 1982). 

A number of researchers have used surface energy libraries to examine the self-assembly of block copolymer species in thin films. It is well known that substrate-block interactions can govern the orientation, wetting symmetry and even the pattern motif of self-assembled domains in block copolymer films [29]. A simple illustration of these effects in diblock copolymer films is shown schematically in Fig. 6. However, for most block copolymer systems the exact surface energy conditions needed to control these effects are unknown, and for many applications of self-assembly (e.g., nanolithography) such control is essential. 

Fig. 6 Illustration of surface energy effects on the self-assembly of thin films of volume symmetric diblock copolymer (a). Sections b and c show surface-parallel block domains orientation that occur when one block preferentially wets the substrate. Symmetric wetting (b) occurs when the substrate and free surface favor interactions with one block B, which is more hydrophobic. Asymmetric wetting (c) occurs when blocks A and B are favored by the substrate and free surface, respectively. For some systems, a neutral substrate surface energy, which favors neither block, results in a self-assembled domains oriented perpendicular to the film plane (d). Lo is the equilibrium length-scale of pattern formation in the diblock system...

Kajava, A. V. (1996). Modeling of a five-stranded coiled coil structure for the assembly domain of the cartilage oligomeric matrix protein. Proteins 24, 218-226. 

Fig. 2.9 a The H-bonds between the PS-P4VP block copolymer and a phenolic resin, b As a result of H-bonding, the phenolic resin and P4VP are confined within the same self-assembled domains as they have microphases separated from the nonpolar PS domains. Crosslinking at elevated temperatures locks the structure, c Depending on the pyrolysis procedure, different pores are created with hydroxyl groups in the pore interior. Reproduced from Ref. [49] by permission of John Wiley Sons Ltd... 

In a next step, the self-assembling properties of the recombinant of S-layer of S. ureae ATCC 13881 are analyzed by in vitro recrystallization experiments on a silicon substrate. To identify the self-assembly domain of this S-layer, three truncation derivatives were created, heterologously expressed in Escherichia coli, purified and their self-assembly investigated. 

Self-assembly of polypeptides via other naturally occurring or de novo designed self-assembling domains such as coiled coUs... 

Polypeptide Materials Based on other Naturally Occurring or De Novo Designed Self-Assembling Domains such as Coiled Coils... 

Clancy L. Mruk K, Archer K et al. Preligand assembly domain-mediated ligand-independent association between TRAIL receptor 4 (TR4) and TR2 regulates TRAIL-induced apoptosis. Proc Natl Acad Sci USA 2005 102(50) 18099-18104. 

Scdger LM, Osvath SR, Xu XM et al. Poxvirus tumor necrosis factor receptor (TNFR)-like T2 proteins contain a conserved preligand assembly domain that inhibits cellular TNFRl-induced cell death. J Virol 2006 80(18) 9300-9309. 

Deng GM, Zheng L, Chan FK et al. Amelioration of inflammatory arthritis by targeting the preligand assembly domain of tumor necrosis factor receptors. Nat Med 2005 11(10) 1066-1072. 

Figure 82 Proposed assembly and the corresponding SAXS curves of symmetric brush (a) random copolymers g(-[PLA-r-P/iBA] and (b) block copolymers g(-[PLA-b-P/iBA]. (inset in b) Photograph of slowly dried 0-[PLA2oo-i-PftBA2oo] showing green color due to reflectance from the large self-assembled domains. Reprinted from Xia, Y. Olsen, B. D. Kornfield, J. A. Grubbs, R. H. J. Am. Chem. Soc. 2009, 131 (51), 18525-18532, with permission from ACS. ...

Haghpanah JS, et al. (2009) Artificial Protein Block Copolymers Blocks Comprising Two Distinct Self-Assembling Domains. Chembiochem. 10 p. 2733-5. 

Fig. 1. Selected dynamin family members in mammals. The three dynamin family members that have been studied in our lab are shown here. Dynamin is involved in vesicular traffic. Drpl contributes to mitochondrial outer membrane division. Opal is localized to the mitochondrial intermembrane space where it affects inner membrane morphology and mitochondrial fusion. All family members have GTPase, Middle, and Assembly domains. Genuine dynamins have a pleckstrin homology (PH) domain and a C-terminal proline rich domain (PRD). Other family members have divergent segments at the N-terminus (Opal) or between the middle domain and GED (black areas in Drpl and Opal). The N-terminus of Opal has a predicted mitochondrial targeting sequence and coiled coil.

Figure 29 Schematics for the switching protonic conductivity based on phase transitions within the hierarchically self-assembled polymer complexes based on PS-fc-P4VP and PDP-I-MSA. SAXS-pattems and DC-conductivity as a function of temperature are shown. The geometry of the conducting self-assembled domains is illustrated. (Reproduced with permission from Ref. 82. American Association for the Advancement of Science, 1998. 82. J. Ruokolainen, R. Makinen, M. Torkkeli, T. Makela, R. Serimaa, G. ten Brinke,...

Figure 6 Molecular model of O2 sensor complex in NEB cell. Shown is the a-jS potassium (K+) channel complex with tetramer of a-subunits forming the ionic pore, -subiuiits interact with the assembly domains T1 in the cytosol. A positively chaiged amino terminal ball domain of the a-subunit (and possibly of the -subunit) underlies fast inactivation. The reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase complex is shown to be associated with this K+-channel complex in NEB cells. Reactive oxygen intermediates produced by the NADPH oxidase modulate the inactivation process by oxidizing specific cysteine residues in the amino terminus, forming disulfide bridges with other cysteines located in the channel and thus immobilizing the inactivation balls. (From Ref 78, Courtesy of Dr. Honore.)...

Chimeric (fusion) proteins that incorporate the R5 peptide have been synthesized to control and precipitate silica nanoparticles. Po Foo and coworkers have utilized a two-component chimeric protein consisting of the R5 polypeptide (from C. fusiformis) and the self-assembling domain based on the consensus repeat in the major ampullate spidroin protein 1 (MaSpl) of Nephila clavipes spider dragline silk [64]. MaSpl forms highly stable P-sheet secondary stmctures that can be spun into intricate fibers which, when fused with the sihca-templating R5-peptide, allow for the formation of film-like and fibrous silica structures (Figure 1.18). 

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