Regulating ferredoxin electron transfer using nanobody and antigen interactions.

ABSTRACT: Fission and fusion can be used to generate new regulatory functions in proteins. This approach has been used to create ferredoxins (Fd) whose cellular electron transfer is dependent upon small molecule binding. To investigate whether Fd fragments can be used to monitor macromolecular binding reactions, we investigated the effects of fusing fragments of Mastigocladus laminosus Fd to single domain antibodies, also known as nanobodies, and their protein antigens. When Fd fragments arising from fission were fused to green fluorescent protein (GFP) and three different anti-GFP nanobodies, split proteins were identified that supported Fd-mediated electron transfer from Fd-NADP reductase (FNR) to sulfite reductase (SIR) in Escherichia coli. However, the order of nanobody and antigen

SUBMITTER: Truong A 

PROVIDER: S-EPMC11886610 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature