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- 1From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-Reviewed
Crystal structures of aprataxin ortholog Hnt3 reveal the mechanism for reversal of 5'-adenylated DNA
Aprataxin is a DNA deadenylase that resolves DNA 5'-AMP termini and reverses abortive DNA ligation. The crystal structures of Schizosaccharomyces pombe aprataxin Hnt3 in its apo form and in complex to dsDNA and... - 2From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedIn contrast to prokaryotic elongation factor EF-Tu, which delivers aminoacyl-tRNAs to the ribosomal A-site, eukaryotic initiation factor eIF2 binds methionyl initiator transfer RNA (Met-[tRNA.sub.i.sup.Met]) to the...
- 3From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedTubulin tyrosine ligase (TTL) catalyzes the post-translational C-terminal tyrosination of [alpha]-tubulin. Tyrosination regulates recruitment of microtubule-interacting proteins. TTL is essential. Its loss causes...
- 4From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedDNA ligases finalize DNA replication and repair through DNA nick-sealing reactions that can abort to generate cytotoxic 5'-adenylation DNA damage. Aprataxin (Aptx) catalyzes direct reversal of 5'-adenylate adducts to...
- 5From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedDuring protein synthesis, mRNA and tRNAs are iteratively translocated by the ribosome. Precisely what molecular event is rate limiting for translocation is not known. Here we show that disruption of the interactions...
- 6From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedTfam (transcription factor A, mitochondrial), a DNA-binding protein with tandem high-mobility group (HMG)-box domains, has a central role in the expression, maintenance and organization of the mitochondrial genome. It...
- 7From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedOrganism-wide RNA interference (RNAi) is due to the transport of mobile silencing RNA throughout the organism, but the identities of these mobile RNA species in animals are unknown. Here, we present genetic evidence...
- 8From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedmiRNA-mediated repression in animals is dependent on the GW182 protein family. GW182 proteins are recruited to the miRNA repression complex through direct interaction with Argonaute proteins, and they function...
- 9From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedmiRNAs recruit the miRNA-induced silencing complex (miRISC), which includes Argonaute and GW182 as core proteins. GW182 proteins effect translational repression and deadenylation of target mRNAs. However, the molecular...
- 10From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedWe have used EM and biochemistry to characterize the structure of NuA4, an essential yeast histone acetyltransferase (HAT) complex conserved throughout eukaryotes, and we have determined the interaction of NuA4 with the...
- 11From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedLow-density-lipoprotein (LDL) receptor-related proteins 5 and 6 (LRP5/6) are Wnt co-receptors essential for Wnt/[beta]-catenin signaling. Dickkopf 1 (DKK1) inhibits Wnt signaling by interacting with the extracellular...
- 12From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedThe microRNA-induced silencing complex (miRISC) protein TNRC6 (also called GW182) uses dispersed tryptophan-containing repeats in unstructured regions to recruit the CCR4-NOT nuclease complex leading to mRNA...
- 13From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedThe archaeal AUA-codon specific [tRNA.sup.Ile] contains 2-agmatinylcytidine ([agm.sup.2]C or agmatidine) at the anticodon wobble position (position 34). The formation of this essential modification is catalyzed by...
- 14From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedThe cytidine at the first position of the anticodon (C34) in the AUA codon-specific archaeal [tRNA.sup.Ile2] is modified to 2-agmatinylcytidine ([agm.sup.2]C or agmatidine), an agmatine-conjugated cytidine derivative,...
- 15From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedBroadly neutralizing antibodies such as 2F5 are directed against the membrane-proximal external region (MPER) of HIV-1 GP41 and recognize well-defined linear core sequences. These epitopes can be engrafted onto protein...
- 16From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedHuman mitochondrial transcription factor A, TFAM, is essential for mitochondrial DNA packaging and maintenance and also has a crucial role in transcription. Crystallographic analysis of TFAM in complex with an...
- 17From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedThe extent to which ligand occupancy and dimerization contribute to erbB1 signaling is controversial. To examine this, we used two-color quantum-dot tracking for visualization of the homodimerization of human erbB1 and...
- 18From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedThe mammalian mitochondrial transcription factor A (TFAM) is encoded in the nucleus and imported into mitochondria, where it functions as an activator of mtDNA transcription and packages mtDNA into DNA-protein...
- 19From: Nature Structural and Molecular Biology. (Vol. 18, Issue 11) Peer-ReviewedThe Saccharomyces cerevisiae proteasome comprises a 19-subunit regulatory particle and a 28-subunit core particle. To be degraded, substrates must cross the core particle-regulatory particle interface, a site for...