Disease relevance of rho

• rho proteins isolated from strains of Escherichia coli with the suA1, suA100, and suA120 polarity suppressor mutant alleles of the rho gene are shown to be defective in termination of T7 DNA transcription in vitro [1].
• Function of the novel subdomain in the RNA binding domain of transcription termination factor Rho from Micrococcus luteus [2].
• Mutants in Escherichia coli transcription termination factor Rho, termed rho(nusD), were previously isolated based on their ability to block the growth of bacteriophage T4 [3].
• Purification of RNA polymerase and transcription-termination factor Rho from Erwinia carotovora [4].
• A protein has been isolated from Bacillus subtilis which has functions similar to that of transcription termination factor rho (rho) from Escherichia coli [5].

High impact information on rho

• Here we show that psu also antagonizes activity of the Escherichia coli transcription termination factor rho at the terminator of the trp operon [6].
• Maximizing gene expression from plasmid vectors containing the lambda PL promoter: strategies for overproducing transcription termination factor rho [7].
• These and other results obtained with mutants defective in transcription termination factor rho suggest the involvement of a rho-sensitive site in the control of sigma gene expression in E. coli [8].
• Escherichia coli transcription termination factor Rho is a ring-shaped hexameric protein that uses the energy derived from ATP hydrolysis to dissociate RNA transcripts from the ternary elongation complex [9].
• Transcription termination factor Rho contains three noncatalytic nucleotide binding sites [10].

Chemical compound and disease context of rho

• Evidence for the location of bicyclomycin binding to the Escherichia coli transcription termination factor Rho [11].
• Fluorescent modification of the cysteine 202 residue of Escherichia coli transcription termination factor rho [12].
• 8-Azido-ATP inactivation of Escherichia coli transcription termination factor Rho. Modification of one subunit inactivates the hexamer [13].
• Transcription termination factor Rho from Micrococcus luteus, a high G + C Gram-positive bacterium, contains an unusual extra sequence within its RNA binding domain that is rich in Arg, Glu, and Asp residues and deficient in hydrophobic residues [2].
• Kinetic studies document that the essential Escherichia coli transcription termination factor rho utilizes Mg(2+) and ATP as a substrate and requires a second Mg(2+) ion for maximum poly(C)-dependent ATP hydrolysis activity [14].

Biological context of rho

• The mechanism of ATP hydrolysis at the noncatalytic sites of the transcription termination factor Rho [15].
• Escherichia coli transcription termination factor rho is a hexamer with three catalytic subunits that turnover ATP at a fast rate and three noncatalytic subunits that turnover ATP at a relatively slow rate [15].
• Addition of the transcription termination factor Rho, a RNA binding protein, to E. coli transcription complexes resulted in RNA crosslinking to Rho and to the beta and beta' subunits of polymerase [16].
• Effects on mRNA degradation by Escherichia coli transcription termination factor Rho and pBR322 copy number control protein Rop [3].
• The mechanism of autoregulation was found to be independent both of transcription termination factor Rho and of the promoter transcribing nusG [17].

Associations of rho with chemical compounds

• The lone cysteine residue (Cys-202) of transcription termination factor rho has been modified with the sulfhydryl-specific dyes 5-iodoacetamidofluorescein and 5-(2-[iodoacetyl)amino)ethyl)aminonaphthalene-1-sulfonic acid [12].
• Enhancement of transcription termination factor rho activity with potassium glutamate [18].
• Effects of bicyclomycin on RNA- and ATP-binding activities of transcription termination factor Rho [19].

Other interactions of rho

• Metabolism of ribosomal RNA in mutants of Escherichia coli doubly defective in ribonuclease III and the transcription termination factor rho [20].

Analytical, diagnostic and therapeutic context of rho

• Specifically, MALDI mass analysis was used to determine the molecular weights of the phage T4 gene 32 protein (gp32) crosslinked to the oligonucleotide (dT)20, and the Escherichia coli transcription termination factor rho, photoaffinity labeled with 4-thio-uridine-diphosphate (4sUDP) [21].

References