Energy Transfer Processes in Bioluminescence

Ward, William W.

doi:10.1007/978-1-4684-3551-1_1

Cited by 43 publications

(17 citation statements)

References 150 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…To determine the subcellular location of Rat9p, we epitope tagged it with GFP. GFP is a 26.9-kDa protein from the jellyfish Aequorea victoria that functions as an in vivo fluorescent molecular tag with spectral properties similar to FITC (Ward, 1979). An in-frame fusion between GFP and RAT9 was constructed and transformed into a RAT9 deletion strain.…”

Section: Resultsmentioning

confidence: 99%

Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p.

Goldstein

Snay

Heath

et al. 1996

MBoC

View full text Add to dashboard Cite

In a screen for mutants defective in nucleocytoplasmic export of mRNA, we have identified a new component of the Saccharomyces cerevisiae nuclear pore complex (NPC). The RAT9/NUP85 (ribonucleic acid trafficking) gene encodes an 84.9-kDa protein that we have localized to NPCs by tagging the RAT9/NUP85 gene with the in vivo molecular marker Green Fluorescent Protein. In cells containinf either the rat9-1 allele or a complete deletion of the RAT9/NUP85 gene, poly(A) RNA accumulates rapidly in nuclei after a shift from 23°C to 37°C. Under these same conditions, rapid fragmentation of the nucleolus was also observed. At the permissive growth temperature in rat9-1 or RAT9 deletion strains, the nuclear envelope (NE) becomes detached from the main body of the nucleus, forming long thin double sheets of NE. NPCs within these sheets are clustered and some appear to be locked together between opposing sheets of NE such that their nucleoplasmic faces are in contact. The Rat9/Nup85 protein could not be detected in cells carrying a mutation of RAT2/NUP120, suggesting that Rat9p/Nup85p cannot be assembled into NPCs in the absence of Rat2p/Nupl2Op. In contrast, Rat9/ Nup85 protein was readily incorporated into NPCs in strains carrying mutant alleles of other nucleoporin genes. The possible role of Rat9p/Nup85p in NE integrity and the loss of nucleoporins when another nucleoporin is mutant or absent are discussed.

show abstract

Section: Resultsmentioning

confidence: 99%

Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p.

Goldstein

Snay

Heath

et al. 1996

MBoC

View full text Add to dashboard Cite

show abstract

“…Green fluorescent proteins exist in a variety of coelenterates, both hydrozoa such as Aequorea, Obelia, and Phialidium, and anthozoa such as Renilla (3,13). In this review, GFP refers to the Aequorea protein except where another genus name is specifically indicated.…”

Section: Occurrence Relation To Bioluminescence and Comparison Withmentioning

confidence: 99%

The Green Fluorescent Protein

Tsien

1998

Annu. Rev. Biochem.

5,673

115

5,075

View full text Add to dashboard Cite

In just three years, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria has vaulted from obscurity to become one of the most widely studied and exploited proteins in biochemistry and cell biology. Its amazing ability to generate a highly visible, efficiently emitting internal fluorophore is both intrinsically fascinating and tremendously valuable. High-resolution crystal structures of GFP offer unprecedented opportunities to understand and manipulate the relation between protein structure and spectroscopic function. GFP has become well established as a marker of gene expression and protein targeting in intact cells and organisms. Mutagenesis and engineering of GFP into chimeric proteins are opening new vistas in physiological indicators, biosensors, and photochemical memories. CONTENTS

show abstract

“…4B) (DeLuca et al, 1971;Hart et al, 1979;Shimomura, 2006). To enable the energy transfer, Renilla luciferase and Renilla GFP are required to form a protein-protein complex (Ward andCormier, 1976, 1978;Ward, 1979), and so luciferase must interact simultaneously with both proteins, CBP and GFP. Despite solid biophysical data on Renilla GFP-Renilla luciferase complexation, no structural information is available for this interaction at the present time.…”

Section: Soft Coral Renillamentioning

confidence: 99%

“…Several lines of evidence indicate that delivery of luciferin from the binding protein to the luciferase as well as modulation of bioluminescence spectra as a result of energy transfer to the antenna proteins, involves protein-protein interactions (Morise et al, 1974;Ward andCormier, 1976, 1978;Nicolas et al, 1991;Cutler, 1995;Schultz et al, 2005;Titushin et al, 2008Titushin et al, , 2010Stepanyuk et al, 2009;. The interactions are of a transient nature, with K D in the range of 10 −6 -10 −3 mol/L, which highly impedes direct detection of the complexes, or their structural studies with Xray crystallography or NMR methods.…”

Section: Introductionmentioning

confidence: 99%

Protein-protein complexation in bioluminescence

et al. 2011

View full text Add to dashboard Cite

In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an "accessory protein" whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an "antenna protein" altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca 2+ -regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of Xray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.

show abstract

Energy Transfer Processes in Bioluminescence

Cited by 43 publications

References 150 publications

Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p.

Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p.

The Green Fluorescent Protein

Protein-protein complexation in bioluminescence

Contact Info

Product

Resources

About