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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Neurochemicals aid bee nestmate recognition

Article Abstract:

The theory of kin selection depends on the discrimination of relatives from non-relatives. The underlying neurobiological mechanisms of this ability have not been studied. Evidence is provided for neurochemical modulation of nestmate recognition. A modification of a laboratory assay measuring the probability that laboratory-reared five day old adult worker honeybees, will be aggressive towards and introduced bee, was used. Bees injected with octopamine agonists were more likely to be aggressive towards non-nestmates.

Author: Robinson, Gene E., Heuser, laura M., LeConte, Yves, Lenquette, Frederic, Hollingworth, Robert M.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
Bees, Kin selection (Evolution), Kin selection (Natural selection)

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'Distorted' RNA helix recognition

Article Abstract:

Cognate synthetase recognizes the free 2-amino group contributed by G of the G-U pair at the third position in the acceptor helix of alanine transfer (t) RNAs. Simple removal of the 2-amino group is sufficient to abolish amino-acylation with alanine. Restoration of the free 2-amino group by substitution of a non-natural base pair restores amino-acylation with alanine. When the free amino group is lacking, the signal for alanylation is due to indirect recognition of a distortion of the RNA helix.

Author: Schimmel, Paul, Musier-Forsyth, Karin
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Analysis, Nucleotides, Aminoacyl-tRNA

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Aminoacylation error correction

Article Abstract:

A connective polypeptide 1 (CP1) region in valyl-tRNA synthetase and isoleucyl-tRNA synthetase deacylates Thr-tRNA(super Val) and Val-tRNA(super Ile) respectively, with high specificity. Isosteric amino acids may get attached to the wrong tRNA which is corrected by the editing activity that deacylates mischarged tRNA. CP1 binds, catalyzes and releases the product after editing. The CP1 segment contains 211 residues and is a stable folded protein with a beta-sheet structure.

Author: Schimmel, Paul, Lin, Laura, Hale, Stephen P.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Reports, Observations, RNA, Aminoacyl-tRNA synthetases

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