Critical role of tyrosine 79 in the fluorescence resonance energy transfer and terbium(III)-dependent self-assembly of ciliate Euplotes octocarinatus centrin

2010 ◽  
Vol 15 (7) ◽  
pp. 995-1007 ◽  
Author(s):  
Lian Duan ◽  
Wen Liu ◽  
Zhi-Jun Wang ◽  
Ai-Hua Liang ◽  
Bin-Sheng Yang
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Self Assembly ◽  
Critical Role ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescence Resonance ◽  
Euplotes Octocarinatus

Dual Role of Blue Luminescent MoS2Quantum Dots in Fluorescence Resonance Energy Transfer Phenomenon

Small ◽  
2014 ◽  
Vol 10 (19) ◽  
pp. 3858-3862 ◽  
Author(s):  
Hyun Dong Ha ◽  
Dong Ju Han ◽  
Jong Seob Choi ◽  
Minsu Park ◽  
Tae Seok Seo
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Dual Role ◽  
Transfer Phenomenon ◽  
Fluorescence Resonance

scholarly journals Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer

2004 ◽  
Vol 166 (7) ◽  
pp. 1015-1025 ◽  
Author(s):  
David Staněk ◽  
Karla M. Neugebauer
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Specific Protein ◽  
Cajal Bodies ◽  
Small Nuclear Ribonucleoprotein ◽  
Fluorescence Resonance ◽  
Nuclear Ribonucleoprotein

Spliceosomal small nuclear ribonucleoprotein particles (snRNPs) are required for pre-mRNA splicing throughout the nucleoplasm, yet snRNPs also concentrate in Cajal bodies (CBs). To address a proposed role of CBs in snRNP assembly, we have used fluorescence resonance energy transfer (FRET) microscopy to investigate the subnuclear distribution of specific snRNP intermediates. Two distinct complexes containing the protein SART3 (p110), required for U4/U6 snRNP assembly, were localized: SART3•U6 snRNP and SART3•U4/U6 snRNP. These complexes segregated to different nuclear compartments, with SART3•U6 snRNPs exclusively in the nucleoplasm and SART3•U4/U6 snRNPs preferentially in CBs. Mutant cells lacking the CB-specific protein coilin and consequently lacking CBs exhibited increased nucleoplasmic levels of SART3•U4/U6 snRNP complexes. Reconstitution of CBs in these cells by expression of exogenous coilin restored accumulation of SART3•U4/U6 snRNP in CBs. Thus, while some U4/U6 snRNP assembly can occur in the nucleoplasm, these data provide evidence that SART3•U6 snRNPs form in the nucleoplasm and translocate to CBs where U4/U6 snRNP assembly occurs.

Fluorescence resonance energy transfer in multifunctional nanofibers designed via block copolymer self-assembly

2019 ◽  
Vol 21 (29) ◽  
pp. 16137-16146 ◽  
Author(s):  
Sajan Singh ◽  
Ajeet Singh ◽  
Mona Mittal ◽  
Rajiv Srivastava ◽  
Sameer Sapra ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Block Copolymer ◽  
Block Copolymers ◽  
Quantum Dot ◽  
Fluorescence Resonance Energy Transfer ◽  
Self Assembly ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescent Dye ◽  
Fluorescence Resonance

We demonstrate the fabrication of multifunctional nanofibers via cooperative self-assembly of block copolymers mixed with a quantum dot (QD) donor and a fluorescent dye acceptor exhibiting interesting FRET behavior.

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