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Malunited distal radius fractures (DRFs) occasionally restrict forearm rotation, but the underlying pathology remains unclear. We aimed to elucidate the mechanism of rotational restriction by retrospective analysis of 23 patients with unilateral malunited DRFs who presented restricted forearm rotation. We conducted computed tomography during forearm rotation on both sides. Three-dimensional (3D) bone surface models of the forearm were created, and 3D deformity of the distal radius, translation of the distal radius relative to the ulna, distal radioulnar joint (DRUJ) contact area, and estimated path length (EPL) of distal radioulnar ligaments (DRUL) during forearm rotation were evaluated. In total, 18 patients had dorsal angular deformities (DA group) and five had volar angular deformities (VA group). In the DA group, the closest point between the distal radius and ulna on DRUJ was displaced to the volar side during supination and pronation (p < 0.001); DRUJ contact area was not significantly different between the DA and normal groups. In bone-ligament model simulation, the EPL of dorsal DRUL was longer in the DA group than in the normal group (p < 0.001); opposite phenomena were observed in the VA group. In the DA group, translation of the distal radius in a volar direction relative to the ulna during pronation was impaired presumably due to dorsal DRUL tightness. Anatomical normal reduction of the distal radius by corrective osteotomy may improve forearm rotation by improving triangular fibrocartilage complex tightness and normalizing translation of the distal radius relative to the ulna. © 2019 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res 37:1881-1891, 2019.

In thermophilic bacteria, specific 2-thiolation occurs on the conserved ribothymidine at position 54 (T54) in tRNAs, which is necessary for survival at high temperatures. T54 2-thiolation is achieved by the tRNA thiouridine synthetase TtuA and sulfur-carrier proteins. TtuA has five conserved CXXC/H motifs and the signature PP motif, and belongs to the TtcA family of tRNA 2-thiolation enzymes, for which there is currently no structural information. In this study, we determined the crystal structure of a TtuA homolog from the hyperthermophilic archeon Pyrococcus horikoshii at 2.1 A resolution. The P. horikoshii TtuA forms a homodimer, and each subunit contains a catalytic domain and unique N- and C-terminal zinc fingers. The catalytic domain has much higher structural similarity to that of another tRNA modification enzyme, TilS (tRNAIle2 lysidine synthetase), than to the other type of tRNA 2-thiolation enzyme, MnmA. Three conserved cysteine residues are clustered in the putative catalytic site, which is not present in TilS. An in vivo mutational analysis in the bacterium Thermus thermophilus demonstrated that the three conserved cysteine residues and the putative ATP-binding residues in the catalytic domain are important for the TtuA activity. A positively charged surface that includes the catalytic site and the two zinc fingers is likely to provide the tRNA-binding site. Proteins 2013; 81:1232–1244. © 2013 Wiley Periodicals, Inc.

In order to terminate the polymerase reaction at a desired position, a caged thymine derivative--4-O-[2-(2-nitrophenyl)propyl]thymine--was incorporated into PCR primers. In the PCR cycles, the elongation of the nascent strand (5'-->3' direction) by polymerase was site-selectively terminated at the 3'-side of T(NPP). Accordingly, predetermined protruding ends were obtained after the removal of the protecting group by short UVA irradiation. Recombinant vectors coding the GFP gene were successfully prepared by direct ligation of these light-assisted cohesive-ending PCR (LACE-PCR) products with scission fragments obtained by use either of restriction enzymes or of artificial restriction DNA cutters and were used for transformation of E. coli.