Search results
Results from the WOW.Com Content Network
TDP-43 is 414 amino acid residues long. It consists of four domains: an N-terminal domain spanning residues 1–76 (NTD) with a well-defined fold that has been shown to form a dimer or oligomer; [6] [7] two highly conserved folded RNA recognition motifs spanning residues 106–176 (RRM1) and 191–259 (RRM2), respectively, required to bind target RNA and DNA; [8] an unstructured C-terminal ...
TDP-43 (Transactive response DNA-binding protein) is a nuclear protein involved in regulating gene expression by binding to and modifying nucleic acids. [43] More specifically, TDP-43 plays critical roles in RNA processing, including splicing, stability, and transport. In healthy cells, TDP-43 is predominantly found in the nucleus.
DNA-binding proteins are proteins that have DNA-binding domains and thus have a specific or general affinity for single- or double-stranded DNA. [ 3 ] [ 4 ] [ 5 ] Sequence-specific DNA-binding proteins generally interact with the major groove of B-DNA , because it exposes more functional groups that identify a base pair .
Mutations in the TDP-43 gene (known as TARBP or TAR DNA-binding protein) are an exceptionally rare cause of FTLD, despite this protein being present in the pathological inclusions of many cases (FTLD-TDP43). [15] However, mutations in TARBP are a more common cause of ALS, which can present with frontotemporal dementia. Since these instances are ...
DNA-binding domains with functions involving DNA structure have biological roles in DNA replication, repair, storage, and modification, such as methylation. [citation needed] Many proteins involved in the regulation of gene expression contain DNA-binding domains. For example, proteins that regulate transcription by binding DNA are called ...
Insulators contain clustered binding sites for sequence specific DNA-binding proteins [1] and mediate intra- and inter-chromosomal interactions. [2] Insulators function either as an enhancer-blocker or a barrier, or both. The mechanisms by which an insulator performs these two functions include loop formation and nucleosome modifications.
For example, acetylation has been seen to increase the activity of some activators through mechanisms such as increasing DNA-binding affinity. [1] On the other hand, ubiquitination decreases the activity of activators, as ubiquitin marks proteins for degradation after they have performed their respective functions.
One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together (dimerize) two DNA binding regions. The DNA binding region comprises a number of basic amino acids such as arginine and lysine. Proteins containing this domain are transcription factors. [1] [2]