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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Structure of eEF3 and the mechanism of transfer RNA release from the E-site

Article Abstract:

The crystal structure of Saccharomyces cerevisiae eEF3 was studied to show that it consists of an amino-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains, with a chromodomain inserted in ABC2. eEF3 uses an entirely new factor binding site near the ribosomal E-site, with the chromodomain likely to stabilize the ribosomal L1 stalk in an open conformation, thus allowing tRNA release.

Author: Spahn, Christian M.T., Pedersen, Jan Skov, Beckmann, Roland, Halic, Mario, Becker, Thomas, Boesen, Thomas, Andersen, Gregers R., Andersen, Christian B.F., Blau, Michael, Anand, Monika, Balar, Bharvi, Mielke, Thorsten, Kinzy, Terri Goss
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
Food preparations, not elsewhere classified, All Other Miscellaneous Food Manufacturing, Brewers' Yeast, Physiological aspects, Transfer RNA, Crystals, Crystal structure, Brewer's yeast, Saccharomyces cerevisiae

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Following the signal sequence from ribosomal tunnel exit to signal recognition particle

Article Abstract:

An ensemble of structures is presented at subnanometre resolution, which reveals the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-signal recognition particle (SRP) complexes. The results have provided the structural basis for understanding the early steps of co-translational protein sorting.

Author: Wild, Klemens, Beckmann, Roland, Halic, Mario, Becker, Thomas, Pool, Martin R., Blau, Michael, Mielke, Thorsten, Sinning, Irmgard
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
Genetic aspects, Ribosomes, Genetic translation, Translation (Genetics)

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Exotoxin A-eEF2 complex structure indicates ADP ribosylation by ribsome mimicry

Article Abstract:

Mono-ADP-ribosylating toxins that modify intracellular proteins are the bacteria that cause diphtheria, whooping cough, cholera and other diseases. The diphtheria toxin makes a good mimic for an effective poison.

Author: Marquez, Victor E., Jorgensen, Rene, Merril, Rod A., Yates Susan P., Schwan, Adrain L., Boesen, Thomas, Andersen, Gregers R.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
United States, Care and treatment, Causes of, Ribosomal proteins, Diphtheria

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Subjects list: United Kingdom, Research
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