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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive

Article Abstract:

The enzyme arginine methylatransferase PRMT6 which catalyses histone H3 arginine 2 (H3R2me2a) was identified to characterize the relationship between H3 lysine 4 (H3K4me3) and H3R2me2a. The findings suggest that mutual antagonism between H3R2 and H3K4 methylation together with MLL-family complexes contribute to the localized patterns of H3H4 tri-methylation of transcriptionally active promoters in mammalian genomes.

Author: Luscher, Bernhard, Amati, Bruno, Cesaroni, Matteo, Martinato, Francesca, Guccione, Ernesto, Bassi, Christian, Casadio, Fabio, Schuchlautz, Henning
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
Genetic aspects, Arginine, Methylation, Lysine, Methyltransferases, Chemical properties

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Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase

Article Abstract:

The crystal structure analysis of the Escherichia coli Eubacterial leucyl/phenylalanyl-tRNA protein transferase (LF-transferase) complex with phenyalanyl adenosine (rA-Phe) is described. The protein-based mechanism for peptide-bond formation by LF-transferase was found to be similar to the reverse reaction of the acylation step observed in the peptide hydrolysis reaction by serine proteases.

Author: Tomita, Kozo, Watanabe, Kazunori, Toh, Yukimatsu, Suto, Kyoko, Shimizu, Yoshihiro, Oka, Natsuhisa, Wada, Takeshi
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
Escherichia coli, Gene expression, Phenylalanine, Peptide bonds

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ClpS is an essential component of the N-end rule pathway in Escherichia coli

Article Abstract:

Study is conducted to show that ClpAP-specific adaptor, ClpS, is essential for degradation of N-end rule substrates by ClpAP in bacteria. Through interaction with this signal, ClpS converts the ClpAP machine into a protease with exquisitely defined specificity, ideally suited to regulatory proteolysis.

Author: Schmidt, R., Erbse, A., Bornemann, T., Schneider-Mergener, J., Mogk, A., Zahn R., Dougan, D.A., Bukau, B.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
United States, Proteolysis

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Subjects list: Research, Physiological aspects, Eukaryotes, Proteases
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