A5091651207- RNA Research and Splicing
- Nuclear Structure and Function
- RNA and protein synthesis mechanisms
- Burkholderia infections and melioidosis
- Research on Leishmaniasis Studies
- RNA modifications and cancer
- Amino Acid Enzymes and Metabolism
- Mesoporous Materials and Catalysis
- Catalytic Processes in Materials Science
- Enzyme Structure and Function
- Biochemical and Molecular Research
California Institute of Technology
2016-2022
University of Sheffield
2011-2022
Blueprint for a macromolecular machine Nuclear pore complexes (NPCs) consist of around 1000 protein subunits, are embedded in the membrane that surrounds nucleus, and regulate transport between nucleus cytoplasm. Although overall shape NPCs is known, details this complex have been obscure. Now, Lin et al. reconstituted components, determined interactions them, fitted them into tomographic reconstruction. Kosinski provided an architectural map inner ring pore. Science , issue pp....
INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are generated by the circumscribed fusion inner outer membranes, pore complexes (NPCs) sole bidirectional gateways for nucleocytoplasmic transport. ~110-MDa human NPC is an ~1000-protein assembly that comprises multiple copies ~34 different proteins, collectively termed nucleoporins. symmetric core...
INTRODUCTION In eukaryotic cells, the selective bidirectional transport of macromolecules between nucleus and cytoplasm occurs through nuclear pore complex (NPC). Embedded in envelope pores, ~110-MDa human NPC is an ~1200-Å-wide ~750-Å-tall assembly ~1000 proteins, collectively termed nucleoporins. Because NPC's eightfold rotational symmetry along nucleocytoplasmic axis, each ~34 different nucleoporins multiples eight. Architecturally, symmetric core composed inner ring encircling central...
The structure of BPSL1549, a protein unknown function from Burkholderia pseudomallei, reveals similarity to Escherichia coli cytotoxic necrotizing factor 1. We found that BPSL1549 acted as potent cytotoxin against eukaryotic cells and was lethal when administered mice. Expression levels bpsl1549 correlate with conditions expected promote or suppress pathogenicity. promotes deamidation glutamine-339 the translation initiation eIF4A, abolishing its helicase activity inhibiting translation. propose name
Abstract The nuclear pore complex (NPC) is the sole bidirectional gateway for nucleocytoplasmic transport. Despite recent progress in elucidating arrangement of structured scaffold building blocks NPC symmetric core, their cohesion by multivalent unstructured linker proteins remained elusive. Combining biochemical reconstitution, high resolution structure determination, docking into cryo-electron tomographic reconstructions, and physiological validation, we elucidated architecture entire...
Abstract The nuclear pore complex (NPC) is the sole bidirectional gateway for nucleocytoplasmic transport. Despite recent progress in elucidating NPC symmetric core architecture, asymmetrically decorated cytoplasmic face, essential mRNA export and a hotspot nucleoporin-associated diseases, has remained elusive. Here, we report composite structure of entire human face obtained by combining biochemical reconstitution, crystal determination, docking into cryo-electron tomographic...
Abstract Burkholderia pseudomallei lethal factor 1 (BLF1) exhibits site-specific glutamine deamidase activity against the eukaryotic RNA helicase, eIF4A, thereby blocking mammalian protein synthesis. The structure of a complex between BLF1 C94S and human eIF4A shows that toxin binds in cleft two RecA-like domains forming interactions with residues from both scissile amide target glutamine, Gln339, adjacent to active site. adopt radically twisted orientation compared other structures nature...