Accepted_test
Transcription factors are proteins that regulate gene expression. One common type of domain found in transcription factors is the C2H2 zinc finger. This type of domain has two β‑strands and an α-helix, which is stabilized by a zinc ion coordinated by two cysteine and two histidine residues. These domains are typically involved in specific DNA binding. However, there is increasing evidence that these domains may also play a role in protein-protein interactions.
In this study, structural data on two protein-interacting N-terminal domains of the C2H2 zinc fingers from Drosophila have been obtained.
The first object was the Chromatin-Linked Adaptor for MSL Proteins (CLAMP). Earlier we demonstrated that CLAMP directly interacts with the male-specific organizer of the complex (MSL2) which plays an important role in the specificity of binding to the X chromosome during the process of dosage compensation in Drosophila. We demonstrated that CLAMP87-153 is a classical C2H2 zinc finger with an unusual ability to interact with its protein partner.
The second object is CG18262. It appears to be a member of a new family of C2H2 zinc fingers. This domain has an additional β-strand at the N‑terminus. We demonstrated that additional β‑strand at the N‑terminus responsible for dimerization.
Our findings will contribute to a better understanding of the processes involved in transcription regulation.