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'Distorted' RNA helix recognition

Paul Schimmel
Karin Musier-Forsyth
Research05 Dec 1996
Nature

Volume: 384, P: 422
Functional contacts of a transfer RNA synthetase with 2′-hydroxyl groups in the RNA minor groove

Karin Musier-Forsyth
Paul Schimmel
Research11 Jun 1992
Nature

Volume: 357, P: 513-515
Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein

HIV-1 replication is inhibited by the enzyme APOBEC3G via two separate mechanisms. A deamination mechanism requires rapid binding and release of single-stranded DNA (ssDNA), whereas a roadblock mechanism requires slow binding. Now APOBEC3G has been shown to initially bind ssDNA with rapid on–off rates. The enzyme subsequently converts via oligomerization to a slowly dissociating binding mode, which, it is proposed, inhibits reverse transcription.

Kathy R. Chaurasiya
Micah J. McCauley
Mark C. Williams
Research24 Nov 2013
Nature Chemistry

Volume: 6, P: 28-33
Publisher Correction: Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid

Youngzee Song
Huihao Zhou
Paul Schimmel
Amendments and CorrectionsOpen Access13 Mar 2018
Nature Communications

Volume: 9, P: 1
Wobble puts RNA on target

Enzymes that attach amino acids to transfer RNAs during protein synthesis must recognize both substrates specifically. Crystal structures reveal a mechanism that explains the RNA specificity for one such system. See Article p.507

Oscar Vargas-Rodriguez
Karin Musier-Forsyth
News & Views11 Jun 2014
Nature

Volume: 510, P: 480-481
Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid

Non-proteinogenic (np) amino acids in the food chain present challenges for the human translation machinery. Here the authors show that, while AlaRS and ProRS activate toxic np azetidine-2-carboxylic acid (Aze) present in sugar beets and lilies, only the AlaRS editing system rejects Aze.

Youngzee Song
Huihao Zhou
Paul Schimmel
ResearchOpen Access22 Dec 2017
Nature Communications

Volume: 8, P: 1-8
Role of zinc ion in translational accuracy becomes crystal clear

Aminoacyl-tRNA synthetases play a central role in assuring a high degree of accuracy in protein synthesis. New high resolution structures of threonyl-tRNA synthetase bound to threonine or a threonyl-adenylate analog reveal how an active site zinc atom contributes to translational fidelity.

Karin Musier-Forsyth
Penny J. Beuning
News & Views01 Jun 2000
Nature Structural Biology

Volume: 7, P: 435-436

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'Distorted' RNA helix recognition

Functional contacts of a transfer RNA synthetase with 2′-hydroxyl groups in the RNA minor groove

Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein

Publisher Correction: Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid

Wobble puts RNA on target

Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid

Role of zinc ion in translational accuracy becomes crystal clear

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