scholarly journals RNA Detection in Live Bacterial Cells Using Fluorescent Protein Complementation Triggered by Interaction of Two RNA Aptamers with Two RNA-Binding Peptides

2011 ◽  
Vol 4 (3) ◽  
pp. 494-508 ◽  
Author(s):  
Hung-Wei Yiu ◽  
Vadim V. Demidov ◽  
Paul Toran ◽  
Charles R. Cantor ◽  
Natalia E. Broude
Keyword(s):  
Rna Binding ◽  
Fluorescent Protein ◽  
Rna Aptamers ◽  
Bacterial Cells ◽  
Rna Detection ◽  
Binding Peptides ◽  
Protein Complementation ◽  
Live Bacterial Cells

RNA visualization in live bacterial cells using fluorescent protein complementation

2007 ◽  
Vol 4 (5) ◽  
pp. 421-427 ◽  
Author(s):  
Maria Valencia-Burton ◽  
Ron M McCullough ◽  
Charles R Cantor ◽  
Natalia E Broude
Keyword(s):  
Fluorescent Protein ◽  
Bacterial Cells ◽  
Protein Complementation ◽  
Live Bacterial Cells

scholarly journals Mex67p of Schizosaccharomyces pombeInteracts with Rae1p in Mediating mRNA Export

2000 ◽  
Vol 20 (23) ◽  
pp. 8767-8782 ◽  
Author(s):  
Jin Ho Yoon ◽  
Dona C. Love ◽  
Anjan Guhathakurta ◽  
John A. Hanover ◽  
Ravi Dhar
Keyword(s):  
Nuclear Export ◽  
Rna Binding ◽  
Fluorescent Protein ◽  
Synthetic Lethality ◽  
Sequence Similarity ◽  
Mrna Export ◽  
Nuclear Periphery ◽  
Nuclear Pore ◽  
Multicopy Suppressor ◽  
Accessory Factor

ABSTRACT We identified the Schizosaccharomyces pombe mex67 gene (spmex67) as a multicopy suppressor of rae1-167 nup184-1 synthetic lethality and the rae1-167 tsmutation. spMex67p, a 596-amino-acid-long protein, has considerable sequence similarity to the Saccharomyces cerevisiae Mex67p (scMex67p) and human Tap. In contrast toscMEX67, spmex67 is essential for neither growth nor nuclear export of mRNA. However, an spmex67 null mutation (Δmex67) is synthetically lethal with therae1-167 mutation and accumulates poly(A)+ RNA in the nucleus. We identified a central region (149 to 505 amino acids) within spMex67p that associates with a complex containing Rae1p that complements growth and mRNA export defects of therae1-167 Δmex67 synthetic lethality. This region is devoid of RNA-binding, N-terminal nuclear localization, and the C-terminal nuclear pore complex-targeting regions. The (149–505)-green fluorescent protein (GFP) fusion is found diffused throughout the cell. Overexpression of spMex67p inhibits growth and mRNA export and results in the redistribution of the diffused localization of the (149–505)-GFP fusion to the nucleus and the nuclear periphery. These results suggest that spMex67p competes for essential mRNA export factor(s). Finally, we propose that the 149–505 region of spMex67p could act as an accessory factor in Rae1p-dependent transport and that spMex67p participates at various common steps with Rae1p export complexes in promoting the export of mRNA.

Real-time monitoring and inhibition of the activity of carbapenemase in live bacterial cells: application to screening of β-lactamase inhibitors

2020 ◽  
Vol 44 (46) ◽  
pp. 20334-20340
Author(s):  
Han Gao ◽  
Ying Ge ◽  
Min-Hao Jiang ◽  
Cheng Chen ◽  
Le-Yun Sun ◽  
...  
Keyword(s):  
Antibiotic Resistance ◽  
Real Time ◽  
Bacterial Cells ◽  
Real Time Monitoring ◽  
Live Bacterial Cells

Antibiotic resistance mediated by β-lactamases including metallo-β-lactamases (MβLs) has become an emerging threat.

scholarly journals Sequence analysis of an artificial family of RNA-binding peptides

2009 ◽  
Vol 11 (11) ◽  
pp. 2688-2696 ◽  
Author(s):  
Jeffrey E. Barrick ◽  
Richard W. Roberts
Keyword(s):  
Sequence Analysis ◽  
Rna Binding ◽  
Binding Peptides

scholarly journals The Subcellular Localization and Functional Analysis of Fibrillarin2, a Nucleolar Protein inNicotiana benthamiana

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Luping Zheng ◽  
Jinai Yao ◽  
Fangluan Gao ◽  
Lin Chen ◽  
Chao Zhang ◽  
...  
Keyword(s):  
Rna Binding ◽  
Fluorescent Protein ◽  
Yellow Fluorescent Protein ◽  
3D Structure ◽  
Nucleolar Protein ◽  
Cajal Body ◽  
Virus Induced Gene Silencing ◽  
Rich Domain ◽  
Organ Deformation ◽  
Localization Signal

Nucleolar proteins play important roles in plant cytology, growth, and development. Fibrillarin2 is a nucleolar protein ofNicotiana benthamiana(N. benthamiana). Its cDNA was amplified by RT-PCR and inserted into expression vector pEarley101 labeled with yellow fluorescent protein (YFP). The fusion protein was localized in the nucleolus and Cajal body of leaf epidermal cells ofN. benthamiana. TheN. benthamianafibrillarin2 (NbFib2) protein has three functional domains (i.e., glycine and arginine rich domain, RNA-binding domain, andα-helical domain) and a nuclear localization signal (NLS) in C-terminal. The protein 3D structure analysis predicted that NbFib2 is anα/βprotein. In addition, the virus induced gene silencing (VIGS) approach was used to determine the function of NbFib2. Our results showed that symptoms including growth retardation, organ deformation, chlorosis, and necrosis appeared in NbFib2-silencedN. benthamiana.

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