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The ABC protein ABCE1, formerly named RNase L inhibitor RLI1, is one of the most conserved proteins in evolution and is expressed in all organisms except eubacteria. Because of its fundamental role in translation initiation and/or ribosome biosynthesis, ABCE1 is essential for life. Its molecular mechanism has, however, not been elucidated. In addition to(More)
Uncoating of clathrin-coated vesicles requires the J-domain protein auxilin for targeting hsc70 to the clathrin coats and for stimulating the hsc70 ATPase activity. This results in the release of hsc70-complexed clathrin triskelia and concomitant dissociation of the coat. To understand the complex role of auxilin in uncoating and clathrin assembly in more(More)
The removal of the clathrin coat is essential for vesicle fusion with acceptor membranes. Disassembly of the coat involves hsc70, which is specifically recruited by members of the auxilin protein family to clathrin lattices. In vitro, this function of auxilin does not require the globular amino-terminal domain of the clathrin heavy chain, which is known to(More)
The crenarchaeal Acidianus two-tailed virus (ATV) undergoes a remarkable morphological development, extracellularly and independently of host cells, by growing long tails at each end of a spindle-shaped virus particle. Initial work suggested that an intermediate filament-like protein, p800, is involved in this process. We propose that an additional(More)
Clathrin light chains (CLCs) are regulatory subunits of clathrin triskelia. Based on homology searches in Arabidopsis thaliana data bases we have identified three putative CLC clones, and have focused on the one with the highest homology to mammalian CLC sequences. Analysis of its sequence has revealed coiled-coil structures within a region that corresponds(More)
The two structural domains of p529, a predicted AAA ATPase of Acidianus two-tailed virus (ATV), were expressed and purified. The N-terminal domain was demonstrated by loss-of-function mutations to carry ATPase activity with a temperature optimum of 60°C. This domain also showed DNA binding activity that was stronger for the whole protein and was weakened in(More)
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