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Current Protocols · 2025 ·Vol. 5 ·期 5 ·e70151 · IF 2.2

Co-Expression and Purification of the Complex of Single-Chain H2B-H2A.Z and Histone Chaperone YL1

Yue Liu,Wansen Tan,Jingjun Hong

Chromatin remodeling serves as a critical mechanism for gene regulation, enabling the replacement of canonical histones with their variants through the assistance of histone chaperones. Our study focused on the process by which the histone variant H2A.Z replaces H2A, mediated by the mammalian SRCAP chromatin remodeling complex subunit hYL1. Previous approaches typically involved separately expressing the two proteins and validating their interaction in vitro . In contrast, we designed an artificial single-chain hH2B-hH2A.Z (hTBZ) construct, co-transformed the hYL1 gene with hTBZ, and co-expressed the proteins in E. coli BL21(DE3). We then performed purification, fast protein liquid chromatography (FPLC), and SDS-PAGE analysis. This approach successfully yielded the complexed proteins, confirming the in vivo interaction between hYL1 and hTBZ. © 2025 Wiley Periodicals LLC. Basic Protocol : Co-transformation of hTBZ/YL1 into BL21 (DE3) competent cells, followed by induction and acquisition of protein

CAS / MDL: 110-18-9 329-98-6 367-93-1 60-00-4 637-50-3 7727-54-0

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Current Protocols · 2025 ·Vol. 5 ·期 12 ·e70284 · IF 2.2

Fermentation and Purification of Recombinant Human Type III Collagen Expressed in Escherichia coli

Jinwei Zhai,Wansen Tan,Lei Ji,Jingjun Hong

This article mainly describes a fermentation and purification method for expressing recombinant collagen protein in Escherichia coli . The method comprises constructing engineered bacteria expressing human type III collagen and adopting a strategy of feeding in batches for high-density fermentation. The rapid proliferation of bacterial cells is promoted at 37°C, and then the culture is inoculated into a fermentation tank with different carbon sources for growth. When glycerol is used as the main carbon source, the yield of recombinant collagen protein can reach 0.25 to 0.40 g/L. The method allows exploration of the differences in recombinant collagen production with different carbon sources in order to identify the most suitable fermentation medium component. The human type III collagen produced by the method has the typical structure of collagen, with high cell adhesion and the stability of tissue structure. Therefore, it can be used as the raw material for various collagen products, especially facial fillers, dressings, freeze-dried fibers, and gels. © 2025 Wiley Periodicals LLC. Basic Protocol : Fermentation and purification of recombinant human type III collagen expressed in Escherichia coli

CAS / MDL: 10034-99-8 110-18-9 329-98-6 367-93-1 637-50-3 7727-54-0

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