Single-molecule force measurement via optical tweezers reveals different kinetic features of two BRaf mutants responsible for cardio-facialcutaneous (CFC) syndrome: errata Cheng Wen,1,2,5 Chae-Seok Lim,3,5 Anpei Ye,1,* and J. Julius Zhu3,4 1
Key Laboratory for the Physics & Chemistry of Nano-devices, School of Electronic Engineering & Computer Science, Peking University, Beijing 100871, China 2 School of Lifescience, Peking University, Beijing 100871, China 3 Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA 4 Department of Neuroscience, University of Virginia School of Medicine, Charlottesville, VA 22908, USA 5 These authors contribute equally * [email protected]
Abstract: We correct the omission of the construct and protein purification method in our recent paper [Biomed. Opt. Express 4(12), 2835–2845 (2013)]. © 2014 Optical Society of America OCIS codes: (170.0170) Medical optics and biotechnology; (170.1420) Biology; (170.4520) Optical confinement and manipulation; (350.4855) Optical tweezers or optical manipulation.
References and links 1. 2. 3.
C. Wen, A. Ye, A. Ye, and J. J. Zhu, “Single-molecule force measurement via optical tweezers reveals different kinetic features of two BRaf mutants responsible for cardio-facial-cutaneous (CFC) syndrome,” Biomed. Opt. Express 4(12), 2835–2845 (2013). Y. Qin, Y. Zhu, J. P. Baumgart, R. L. Stornetta, K. Seidenman, V. Mack, L. van Aelst, and J. J. Zhu, “Statedependent Ras signaling and AMPA receptor trafficking,” Genes Dev. 19(17), 2000–2015 (2005). A. Kielland, G. Bochorishvili, J. Corson, L. Zhang, D. L. Rosin, P. Heggelund, and J. J. Zhu, “Activity patterns govern synapse-specific AMPA receptor trafficking between deliverable and synaptic pools,” Neuron 62(1), 84– 101 (2009).
We add the construct and protein purification method mistakenly omitted in our recent paper [1]. The constructs were made following our previous studies [2, 3]. In brief, GST tagged Ras binding domain (RBD) and cysteine rich domain (CRD) expression constructs were generated by subcloning the two domains (amino acids 136-298) of wildtype or mutant human BRaf into pGEX4T-1 (GST-fusion vector, GE Healthcare). GST-RBD-CRD fusion proteins were induced in XL10-Gold E. coli strain (#200314, Stratagene), purified using Glutathione Sepharose 4B (#17-0756-01, GE Healthcare), and concentrated with Amicon Ultra centrifugal filters (Ultracel-30K, Millipore). Hexahistidine (His)-tagged Ras(WT) expression constructs were made by subcloning PCR-amplified full-length human H-Ras into pET28a( + ) (His-tag vector, Novagen). His-tagged Ras(WT) proteins were induced in BL21-CodonPlus (DE3)RILP strain (#230280, Agilent Technologies), purified using Ni-NTA His-Bind Purification Kit (#70751-3, EMD Millipore Novagen), and quantified by Bradford assay kit (Bio-Rad).
#228399 - $15.00 USD Received 4 Dec 2014; published 22 Dec 2014 (C) 2014 OSA 1 Jan 2015 | Vol. 6, No. 1 | DOI:10.1364/BOE.6.000244 | BIOMEDICAL OPTICS EXPRESS 244
Key Laboratory for the Physics & Chemistry of Nano-devices, School of Electronic Engineering & Computer Science, Peking University, Beijing 100871, China 2 School of Lifescience, Peking University, Beijing 100871, China 3 Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA 4 Department of Neuroscience, University of Virginia School of Medicine, Charlottesville, VA 22908, USA 5 These authors contribute equally * [email protected]
Abstract: We correct the omission of the construct and protein purification method in our recent paper [Biomed. Opt. Express 4(12), 2835–2845 (2013)]. © 2014 Optical Society of America OCIS codes: (170.0170) Medical optics and biotechnology; (170.1420) Biology; (170.4520) Optical confinement and manipulation; (350.4855) Optical tweezers or optical manipulation.
References and links 1. 2. 3.
C. Wen, A. Ye, A. Ye, and J. J. Zhu, “Single-molecule force measurement via optical tweezers reveals different kinetic features of two BRaf mutants responsible for cardio-facial-cutaneous (CFC) syndrome,” Biomed. Opt. Express 4(12), 2835–2845 (2013). Y. Qin, Y. Zhu, J. P. Baumgart, R. L. Stornetta, K. Seidenman, V. Mack, L. van Aelst, and J. J. Zhu, “Statedependent Ras signaling and AMPA receptor trafficking,” Genes Dev. 19(17), 2000–2015 (2005). A. Kielland, G. Bochorishvili, J. Corson, L. Zhang, D. L. Rosin, P. Heggelund, and J. J. Zhu, “Activity patterns govern synapse-specific AMPA receptor trafficking between deliverable and synaptic pools,” Neuron 62(1), 84– 101 (2009).
We add the construct and protein purification method mistakenly omitted in our recent paper [1]. The constructs were made following our previous studies [2, 3]. In brief, GST tagged Ras binding domain (RBD) and cysteine rich domain (CRD) expression constructs were generated by subcloning the two domains (amino acids 136-298) of wildtype or mutant human BRaf into pGEX4T-1 (GST-fusion vector, GE Healthcare). GST-RBD-CRD fusion proteins were induced in XL10-Gold E. coli strain (#200314, Stratagene), purified using Glutathione Sepharose 4B (#17-0756-01, GE Healthcare), and concentrated with Amicon Ultra centrifugal filters (Ultracel-30K, Millipore). Hexahistidine (His)-tagged Ras(WT) expression constructs were made by subcloning PCR-amplified full-length human H-Ras into pET28a( + ) (His-tag vector, Novagen). His-tagged Ras(WT) proteins were induced in BL21-CodonPlus (DE3)RILP strain (#230280, Agilent Technologies), purified using Ni-NTA His-Bind Purification Kit (#70751-3, EMD Millipore Novagen), and quantified by Bradford assay kit (Bio-Rad).
#228399 - $15.00 USD Received 4 Dec 2014; published 22 Dec 2014 (C) 2014 OSA 1 Jan 2015 | Vol. 6, No. 1 | DOI:10.1364/BOE.6.000244 | BIOMEDICAL OPTICS EXPRESS 244
