A primitive enzyme for a primitive cell: the protease required for excystation of giardia

Article Abstract:

The effect of a specific cysteine enzyme protease inhibitor on excystation of Giardia was analyzed by incubation of Giardia muris fecal cysts with peptidyl fluoromethyl ketone morpholine-tyrosine (o-methyl)homophenylalanine fluoromethyl ketone (Mu-Tyr(Ome)-hPhe-FMK) at 7-100uM. Excystation was arrested by the cysteine protease inhibitor E-64. However, the enzyme reportedly has no effect on trophozoite motility and replication. Furthermore, enzyme protease activity was localized in cytoplasmic vacuoles by using fluorescent microscopy.

Development and progression, Genetic aspects, Pathogenic microorganisms, Microbial mutation, Gene amplification, Protozoa, Protozoans, Protozoa, Pathogenic

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CDK-independent activation of estrogen receptor by cyclin D1

Article Abstract:

Cyclin D1 acts as a cyclin-dependent kinases (CDK)-independent activator of the estrogen receptor. This novel role for cyclin D1 in growth regulation of estrogen-responsive tissues is carried out by potentiating transcription of estrogen receptor-regulated genes. Cyclin D1 is observed to mediate this activation independent of complex formation to a CDK partner and activates estrogen receptor-mediated transcription in the absence of estrogen and enhances transcription in its presence. This activation is not inhibited by anti-estrogens.

Analysis, Cell cycle, Protein kinases, Estrogen, Estrogen receptors

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The adenovirus protease is activated by a virus-coded disulphide-linked peptide

Article Abstract:

The mechanism of activation of adenovirus protease was investigated. Protease activity could be reconstituted by the presence of a factor from purified virions. Characterization of the isolated factor indicated that it is a 11 amino acid peptide derived from the C-terminus of the structural protein, pVI (pVI-CT). The mechanism of activation involves a thiol-disulphide exchange which is associated with the cysteine residue in pVI-CT.

Adenoviruses

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