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Pisces3rule

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F which DI can interact with the transcriptional repressors TOPLESS (TPL)(Szemenyei et al., 2008), while DII contains the degron motif, and is required for interaction with TIR1 (Dharmasiri et al., 2005a; Kepinski and Leyser, 2005). DIII and DIV facilitate oligomerization with Aux/IAA and ARF proteins (Ulmasov et al., 1997; Ouellet et al., 2001; Nanao et al. 2014). Remarkably, studies on IAA7 usin
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Hment, root and flower development, aberrant male meiotic progression and male sterility, as well as embryogenesis (Zhao et al., 1999; Zhao et al., 2003; Liu et al., 2004; Wang and Yang, 2006; Li et al., 2012). Consequently, the best approach to dissect the diverse roles of SCF complexes is given by studying the function of subgroups of F-box proteins and their individual members. In the following
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Complex, the cullin brings the F-box and E2 moieties into close proximity of around 50A to facilitate transfer of UBQs to a substrate (Zheng et al., 2002b). Skp1-like proteins contain an N-terminal domain fold of around 125 amino acids, which is similar to a BTB/POZ (Broad complex, Tramtrack, Bric-a-brac/Pox virus and Zinc finger) domain (Schulman et al., 2000), and is used by Skp1 to interact wit
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Complex, the cullin brings the F-box and E2 moieties into close proximity of around 50A to facilitate transfer of UBQs to a substrate (Zheng et al., 2002b). Skp1-like proteins contain an N-terminal domain fold of around 125 amino acids, which is similar to a BTB/POZ (Broad complex, Tramtrack, Bric-a-brac/Pox virus and Zinc finger) domain (Schulman et al., 2000), and is used by Skp1 to interact wit
1
Complex, the cullin brings the F-box and E2 moieties into close proximity of around 50A to facilitate transfer of UBQs to a substrate (Zheng et al., 2002b). Skp1-like proteins contain an N-terminal domain fold of around 125 amino acids, which is similar to a BTB/POZ (Broad complex, Tramtrack, Bric-a-brac/Pox virus and Zinc finger) domain (Schulman et al., 2000), and is used by Skp1 to interact wit
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Ullin-repeats. Each of these repeats are composed of a five-helix structural motif in which the helices C to E are organized as a three-helix bundle that interacts with helices A and B to form the cullin repeat (Zheng et al., 2002b). Specifically the first repeat is responsible for binding the substrate adaptor complex of SkpCullin-based Ubiquitin E3 Ligases3 ofand the F-box protein, while the oth
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Ullin-repeats. Each of these repeats are composed of a five-helix structural motif in which the helices C to E are organized as a three-helix bundle that interacts with helices A and B to form the cullin repeat (Zheng et al., 2002b). Specifically the first repeat is responsible for binding the substrate adaptor complex of SkpCullin-based Ubiquitin E3 Ligases3 ofand the F-box protein, while the oth
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Uch larger number of S-PHASE KINASEASSOCIATED PROTEIN 1 (SKP1)-like and F-box proteins exist. Arabidopsis encodes for 21 SKP1-like or ARABIDOPSIS SKIP (ASK)-like proteins (Risseeuw et al., 2003), which can be grouped into two major clades, with ASK1 (At1g10940) to 19 (At2g03160) representing one clade while ASK20 (At2g45950) and ASK21 (At3g61415) comprising the other. This strong clustering of ASK