The unusual active site of Gal6/bleomycin hydrolase can act as a 0 carboxypeptidase, aminopeptidase, and peptide ligase

Article Abstract:

A study was conducted to show that Gal6 protease, of the cysteine peptidases class identified by their ability to inactivate the anti-cancer drug bleomycin, acts as a carboxypeptidase on its C terminus to convert itself to an aminopeptidase and peptide ligase. It was found that the position of the C terminus of Gal6 rather than the sequence of the substrate, determined the substrate specificity of the peptidase activity. A model to explain these diverse activities and Gal6's singular activity to inactivate bleomycin is proposed.

Physiological aspects, Proteases, Ligases

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Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A

Article Abstract:

The crystal structure of the small G protein Rab3A bound to the the effector domain of rabphilin-3A was examined to determine the role of the protein in the regulation of neurotransmitter release. The rabphilin-3A was found to interact with Rab3A in two distinct areas. The first consists of the Rab3A switch I and II regions that are sensitive to the nucleotide-binding state of Rab3A. The second involves a deep pocket in Rab3A that interfaces with SGAWFF structural element of rabphilin-3A.

Research, G proteins, Binding sites (Biochemistry), Active sites (Biochemistry)

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E4F1 is an atypical ubiquitin ligase that modulates p53 effector functions independently of degradation

Article Abstract:

The p53-associated factor E4F1 is identified as an important modulator of the K320 ubiquitylation/acetylation-dependent p53 response. The E4F1 has directed the p53 response toward growth arrest at the expense of apoptosis, which has indicated that E4F1 has played a vital role in the cellular life-or-death decision controlled by p53.

Genetic research, Apoptosis

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