Faculty Opinions recommendation of A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells.

2012 ◽  
Author(s):  
Corey Nislow
Keyword(s):  
Fusion Protein ◽  
Mammalian Cells ◽  
Interacting Proteins ◽  
Biotin Ligase

scholarly journals mSphere of Influence: Where the Pathogen Proteins Are

mSphere ◽  
2021 ◽  
Vol 6 (3) ◽  
Author(s):  
Aaron W. Reinke
Keyword(s):  
Fusion Protein ◽  
Mammalian Cells ◽  
Living Cells ◽  
Host Cells ◽  
Intracellular Pathogens ◽  
Interacting Proteins ◽  
Biotin Ligase ◽  
Link Type ◽  
Cell Biol

ABSTRACT Aaron Reinke studies microsporidian evolution and how microsporidia interact with their hosts. In this mSphere of Influence article, he reflects on how the papers “A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells” (K. J. Roux, D. I. Kim, M. Raida, and B. Burke, J Cell Biol 196:801–810, 2012, https://doi.org/10.1083/jcb.201112098) and “Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging” (H.-W. Rhee, P. Zou, N. D. Udeshi, J. D. Martell, et al., Science 339:1328–1331, 2013, https://doi.org/10.1126/science.1230593) impacted his thinking on how to determine where proteins from intracellular pathogens are located within host cells.

The suitability and application of a GFP-actin fusion protein for long-term imaging of the organization and dynamics of the cytoskeleton in mammalian cells

1998 ◽  
Vol 77 (2) ◽  
pp. 81-90 ◽  
Author(s):  
Axel Choidas ◽  
Andreas Jungbluth ◽  
Antonio Sechi ◽  
John Murphy ◽  
Axel Ullrich ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Mammalian Cells

scholarly journals A programmable Cas9-serine recombinase fusion protein that operates on DNA sequences in mammalian cells

2016 ◽  
pp. gkw707 ◽  
Author(s):  
Brian Chaikind ◽  
Jeffrey L. Bessen ◽  
David B. Thompson ◽  
Johnny H. Hu ◽  
David R. Liu
Keyword(s):  
Fusion Protein ◽  
Dna Sequences ◽  
Mammalian Cells ◽  
Serine Recombinase

Identification of chikungunya virus interacting proteins in mammalian cells

2014 ◽  
Vol 39 (3) ◽  
pp. 389-399 ◽  
Author(s):  
Mandar S Paingankar ◽  
Vidya A Arankalle
Keyword(s):  
Mammalian Cells ◽  
Chikungunya Virus ◽  
Interacting Proteins

scholarly journals Functional Studies of MLL-AF4 and a Murinized pSer-variant thereof: MLL-AF4 Impairs the Ribosome Biosynthesis Pathway

2021 ◽  
Author(s):  
Anna Lena Siemund ◽  
Eric Kowarz ◽  
Rolf Marschalek
Keyword(s):  
Transcription Factor ◽  
Fusion Protein ◽  
Mammalian Cells ◽  
Biological Activities ◽  
Intracellular Localization ◽  
Biological Behavior ◽  
Hematopoietic Stem ◽  
Functional Studies ◽  
Pol I ◽  
Transcription Factor Complex

Abstract Background: Recent pathomolecular studies on the MLL-AF4 fusion protein revealed that the murinized version of MLL-AF4, the MLL-Af4 fusion protein, was able to induce leukemia when expressed in murine or human hematopoietic stem/progenitor cells (1). In parallel, a group from Japan demonstrated that the pSer domain of the AF4 protein, as well as the pSer domain of the MLL-AF4 fusion is able to bind the Pol I transcription factor complex SL1 (2).Here, we investigated the human MLL-AF4 and a pSer-murinized version thereof for their functional properties in mammalian cells. Gene expression profiling studies were complemented by intracellular localization studies and functional experiments concerning the biological activities in the nuecleolus.Results: Based on our results, we have to conclude that MLL-AF4 is predominantly localizing in the nucleolus, thereby interfering withPol I transcription, and subsequently,also ribosomebiogenesis. The murinized pSer-variant is more localizing in the nucleus, which may explain their different biological behavior. Of note, AF4-MLL is cooperating at the molecular level with MLL-AF4, but not with the pSer-murinized version of it.Conclusion: This study provides new insights and a molecular explanation for the known differences between hMLL-hAF4 (not leukemogenic) and hMLL-mAf4 (leukemogenic). While the human pSer domain is able to efficiently recruit the SL1 transcription factor complex, the murine counterpart is not. This has several consequences for our understanding of t(4;11) leukemia which is by far the most frequent leukemia in infants, childhood and adults suffering from MLL-r acute leukemia.

scholarly journals A TAT–streptavidin fusion protein directs uptake of biotinylated cargo into mammalian cells

2005 ◽  
Vol 18 (3) ◽  
pp. 147-152 ◽  
Author(s):  
Brian Albarran ◽  
Richard To ◽  
Patrick S. Stayton
Keyword(s):  
Fusion Protein ◽  
Mammalian Cells

scholarly journals A glycosylated peptide in the West Nile virus envelope protein is immunogenic during equine infection

2008 ◽  
Vol 89 (12) ◽  
pp. 3063-3072 ◽  
Author(s):  
Jody Hobson-Peters ◽  
Philip Toye ◽  
Melissa D. Sánchez ◽  
Katharine N. Bossart ◽  
Lin-Fa Wang ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Fusion Protein ◽  
Synthetic Peptides ◽  
Mammalian Cells ◽  
Protein Glycosylation ◽  
The West ◽  
West Nile ◽  
High Sequence Identity ◽  
Recombinant Peptide ◽  
E Protein

Using a monoclonal antibody directed to domain I of the West Nile virus (WNV) envelope (E) protein, we identified a continuous (linear) epitope that was immunogenic during WNV infection of horses. Using synthetic peptides, this epitope was mapped to a 19 aa sequence (WN19: E147–165) encompassing the WNV NY99 E protein glycosylation site at position 154. The inability of WNV-positive horse and mouse sera to bind the synthetic peptides indicated that glycosylation was required for recognition of peptide WN19 by WNV-specific antibodies in sera. N-linked glycosylation of WN19 was achieved through expression of the peptide as a C-terminal fusion protein in mammalian cells and specific reactivity of WNV-positive horse sera to the glycosylated WN19 fusion protein was shown by Western blot. Additional sera collected from horses infected with Murray Valley encephalitis virus (MVEV), which is similarly glycosylated at position E154 and exhibits high sequence identity to WNV NY99 in this region, also recognized the recombinant peptide. Failure of most WNV- and MVEV-positive horse sera to recognize the epitope as a deglycosylated fusion protein confirmed that the N-linked glycan was important for antibody recognition of the peptide. Together, these results suggest that the induction of antibodies to the WN19 epitope during WNV infection of horses is generally associated with E protein glycosylation of the infecting viral strain.

Sign in / Sign up

Export Citation Format

Share Document