ArticleJournal of the American Chemical Society2007
Phage display evolution of a peptide substrate for yeast biotin ligase and application to two-color quantum dot labeling of cell surface proteins.
Article in Journal of the American Chemical Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 75 citations in OpenAlex.
- Library-on-Library Intercellular Labeling for Selection of Biotin Ligase and Acceptor Peptides.Chembiochem : a European journal of chemical biology · 2026Article
- Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation.Proteins · 2024Review
- Expanding the Chemical Diversity of Genetically Encoded Libraries.ACS combinatorial science · 2020Article
- Molecular Sensing with Host Systems for HyperpolarizedMolecules (Basel, Switzerland) · 2020Review
- A bacterial display system for effective selection of protein-biotin ligase BirA variants with novel peptide specificity.Scientific reports · 2019Article
- Breaking the color barrier - a multi-selective antibody reporter offers innovative strategies of fluorescence detection.Journal of cell science · 2017Article
- Article
- Biomolecular engineering for nanobio/bionanotechnology.Nano convergence · 2017Review
- Rapid isolation and single-molecule analysis of ribonucleoproteins from cell lysate by SNAP-SiMPull.RNA (New York, N.Y.) · 2015Article
- Advances in chemical labeling of proteins in living cells.Cell and tissue research · 2015Review
- Beyond phage display: non-traditional applications of the filamentous bacteriophage as a vaccine carrier, therapeutic biologic, and bioconjugation scaffold.Frontiers in microbiology · 2015Review
- Chemical strategies for the covalent modification of filamentous phage.Frontiers in microbiology · 2014Review
- Investigating bioconjugation by atomic force microscopy.Journal of nanobiotechnology · 2013Review
- Nanoscale bacteriophage biosensors beyond phage display.International journal of nanomedicine · 2013Review
- Article
- Detection of protein-protein interactions using nonimmune IgG and BirA-mediated biotinylation.BioTechniques · 2010Article
- AMPA receptors and synaptic plasticity: a chemist's perspective.Nature chemical biology · 2010Review
- The switch regulating transcription of the Escherichia coli biotin operon does not require extensive protein-protein interactions.Chemistry & biology · 2010Article
- Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase.Journal of the American Chemical Society · 2009Article
- Noncovalent immobilization of streptavidin on in vitro- and in vivo-biotinylated bacterial magnetic particles.Applied and environmental microbiology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Site-specific protein labeling with Escherichia coli biotin ligase (BirA) has been used to introduce fluorophores, quantum dots (QDs), and photocross-linkers onto recombinant proteins fused to a 15-amino acid acceptor peptide (AP) substrate for BirA and expressed on the surface of living mammalian cells. Here, we used phage display to engineer a new and orthogonal biotin ligase-AP pair for site-specific protein labeling. Yeast biotin ligase (yBL) does not recognize the AP, but we discovered a new 15-amino acid substrate for yBL called the yeast acceptor peptide (yAP), using two generations of phage display selection from 15-mer peptide libraries. The yAP is not recognized by BirA, and thus, we were able to specifically label AP and yAP fusion proteins coexpressed in the same cell with differently colored QDs. We fused the yAP to a variety of recombinant proteins and demonstrated biotinylation by yBL at the N-terminus, C-terminus, and within a flexible internal region. yBL is extremely sequence-specific, as endogenous proteins on the surface of yeast and HeLa cells are not biotinylated. This new methodology expands the scope of biotin ligase labeling to two-color imaging and yeast-based applications.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.