The N-terminal region interacts with RNAP (PubMed:21922055). The central region is composed of 3 RNA binding domains, S1, KH 1 and KH 2. The C-terminal region contains 2 acidic repeats, AR1 and AR2, which bind to protein N from phage lambda during antitermination. AR2 interacts with SuhB and RNAP alpha subunit C-terminal domain (rpoA); AR2 cannot bind to both simultaneously (PubMed:31020314, PubMed:31127279). SuhB, NusG and the alpha-CTD of RNAP all interact with the AR2 domain and can displace the AR2 domain from the SSK domain (S1, KH1 and KH2) of NusA (PubMed:31127279).
Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis (PubMed:32871103). Participates in both transcription termination and antitermination. Involved in a variety of cellular termination and antitermination processes, such as Rho-dependent transcriptional termination and intrinsic termination (PubMed:31020314). Domain AR2 interacts with a large number of other proteins and may serve as a platform to recruit these factors for transcriptional regulation (PubMed:31127279). Involved in phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription.
Belongs to the NusA family.
b3169, JW3138, nusA, Transcription termination/antitermination protein NusA, N utilization substance protein A, Transcription termination/antitermination L factor
Proteins
54871Da
We found 1 product in 1 category