Disease relevance of RDBP

• NELF-A has sequence similarity to hepatitis delta antigen (HDAg), the viral protein that binds to and activates RNAPII, whereas NELF-E is an RNA-binding protein whose RNA-binding activity is critical for NELF function [1].
• Moreover, COBRA1 regulation of TFF1 in gastric cancer cells was independent of NELF-E [2].
• Structural studies on the RNA-recognition motif of NELF E, a cellular negative transcription elongation factor involved in the regulation of HIV transcription [3].

High impact information on RDBP

• NELF is composed of five polypeptides, the smallest of which is identical to RD, a putative RNA-binding protein of unknown function [4].
• NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation [4].
• After trained with ribosomal RNA sequences of the RDP (Ribosomal Database Project) database, the system can classify query sequences into more than one hundred phylogenetic classes with a 100% accuracy at a rate of less than 0.3 CPU second per sequence on a workstation [5].
• cDNA cloning and characterization of the protein encoded by RD, a gene located in the class III region of the human major histocompatibility complex [6].
• Western blot analysis and immunoprecipitation of lysates of biosynthetically labelled HeLa cells indicated that RD is a 44 kDa nuclear protein [6].

Biological context of RDBP

• RD, which codes for a putative RNA binding protein, is 205 bp downstream of Bf [7].
• RD and Ski2w proteins may be related to RNA splicing, RNA turnover and regulation of translation [8].
• Structure of the human RD gene: a highly conserved gene in the class III region of the major histocompatibility complex [9].
• We cloned and determined the DNA sequence of a novel gene (termed RD or D6S45) situated in the class III region of the human major histocompatibility complex (HLA) between the Bf and C4A complement genes [9].
• It was of note that DDX13 and RD are in such proximity that their 5' regulatory regions overlap [10].

Associations of RDBP with chemical compounds

• Four ubiquitously expressed genes, RD (D6S45)-SKI2W (SKIV2L)-DOM3Z-RP1 (D6S60E), are present between complement component genes factor B and C4 in the class III region of the HLA [7].
• It has an RNA recognition motif and 24 copies of Arg-Asp (RD) repeats [11].
• The RD protein contains a 60-amino acid (aa) tract consisting almost entirely of alternating basic and acidic aa, (RD)n, primarily arginine (Arg; R) and aspartic acid (Asp; D) [12].
• OBJECTIVE: To isolate a homogeneous polysaccharide RP from RDP (a crude polysaccharide from Dioscorea opposita Thunb.), and study its preliminary com-position and structure [13].

Other interactions of RDBP

• The RD and DDX13 genes were oppositely oriented, and their first exons were overlapped [10].

Analytical, diagnostic and therapeutic context of RDBP

• Fluorescence equilibrium titrations with fluorescently labelled double- and single-stranded oligoribonucleotides representing the TAR RNA stem imply that NELF E RRM binds to the single-stranded TAR RNAs with K(d) values in the low-micromolar range [3].
• The aim of the present study was to investigate the effects of autoclave sterilization on properties of RD as related to its use as a barrier membrane in guided tissue regeneration [14].

References