Journal ArticleDOI
Predicting coiled coils from protein sequences
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TLDR
This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.Abstract:
The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.read more
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Characterization of a silicon transporter gene family in Cylindrotheca fusiformis : sequences, expression analysis, and identification of homologs in other diatoms
TL;DR: The isolation and sequence determination of five silicon transporter (SIT) genes from Cylindrotheca fusiformis are reported, and it is proposed that the cell regulates uptake by controlling the amount or location of each.
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Stu2p: A Microtubule-Binding Protein that Is an Essential Component of the Yeast Spindle Pole Body
TL;DR: Results suggest that Stu2p may play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body and to a lesser extent along spindle microtubules.
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With Apologies to Scheherazade: Tails of 1001 Kinesin Motors
TL;DR: The Kinesin SuperFamilies, a chronology of key events and stories, and some of the key players in the development of the superfamilies can be found here.
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CENP-T proteins are conserved centromere receptors of the Ndc80 complex
Alexander Schleiffer,Michael Maier,Gabriele Litos,Fabienne Lampert,Peter Hornung,Karl Mechtler,Stefan Westermann +6 more
TL;DR: It is demonstrated that centromere-binding proteins are highly conserved between budding yeast and humans and how the Ndc80 complex is anchored to centromeres in a manner that couples chromosome movement to spindle dynamics is demonstrated.
Journal ArticleDOI
The Pik - p resistance to Magnaporthe oryzae in rice is mediated by a pair of closely linked CC-NBS-LRR genes
Bin Yuan,Chun Zhai,Wenjuan Wang,Xiaoshan Zeng,Xiaoke Xu,Hanqiao Hu,Hanqiao Hu,Fei Lin,Ling Wang,Qinghua Pan +9 more
TL;DR: The blast resistance gene Pik-p, mapping to the Pik locus on the long arm of rice chromosome 11, was isolated by map-based in silico cloning and revealed that neither KP3 nor KP4 on their own can impart resistance, but that resistance was expressed when both were introduced simultaneously.
References
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Journal ArticleDOI
The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
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Evidence that the leucine zipper is a coiled coil
TL;DR: A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and characterized and associates in the micromolar concentration range to form a very stable dimer of alpha helices with a parallel orientation.
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Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA.
TL;DR: The putative DNA-binding domain of CREB is structurally similar to the corresponding domains in the phorbol ester-responsive c-jun protein and the yeast transcription factor GCN4.
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α‐Helical coiled coils and bundles: How to design an α‐helical protein
Carolyn Cohen,David A.D. Parry +1 more
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A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
TL;DR: The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 Å resolution, is described, and is the first representative of a second class of aminoacyl-tRNA synthet enzyme structures.