Disease relevance of nrdB

• The nrdA and nrdB genes of Escherichia coli and Salmonella typhimurium encode the R1 and R2 proteins that together form an active class I ribonucleotide reductase [1].
• Genetic and morphological characterization of ftsB and nrdB mutants of Escherichia coli [2].
• Group I self-splicing introns are present in the td, nrdB and sunY genes of bacteriophage T4 [3].

High impact information on nrdB

• An open reading frame between nucleotides 6012 and 7139, encoding a 375-amino acid polypeptide with a molecular weight of 43,466, has been identified as the nrdB gene [4].
• Complementation studies with plasmids and a marker rescue study with bacteriophage M13 nrd indicated that ftsB is an allele of nrdB and that the mutation occurs in the region corresponding to nucleotides 6729 to 7032 of the nrdB gene [5].
• The ftsB gene of Escherichia coli is believed to be involved in cell division [2].
• The number of flagella per unit cell length decreased sharply after shifting the culture temperature from 30 degrees to 40 degrees C in the following Ts mutants: ftsC108, ftsD1033, ftsE1181, ftsF1141, ftsG29, ftsZ84, parA110, dnaB42, nrdB, and dnaG [6].
• Our molecular dissection of the nrdB intron also supports the P9.0 and P10 pairings that have been postulated to help form a complex tertiary structure required to give the RNA sequence its catalytic activity: particularly 3' splice site selection, cleavage and exon ligation [7].

Biological context of nrdB

• The nrdB gene, which encodes the B2 subunit of Escherichia coli ribonucleotide reductase (EC 1.17.4.1), was cloned into multicopy plasmid pSPS2 [8].
• Furthermore, exon sequences flanking sites where introns are inserted in the T4 td, sunY and nrdB genes were determined for all the different T-even isolates studied [3].

Associations of nrdB with chemical compounds

• A temperature-sensitive, salt-rescuable ftsB cell division mutant, MFT84, was found to be hydroxyurea sensitive on low-salt medium [5].

Analytical, diagnostic and therapeutic context of nrdB

• Sequence analysis of a fragment amplified by polymerase chain reaction located the inaA1::lac fusion joint within an open reading frame 311 nucleotides downstream of nrdB, transcribed in the opposite direction, encoding a 168-amino-acid polypeptide [9].
• Functional and sequence analysis of splicing defective nrdB mutants of bacteriophage T4 reveal new bases and a new sub-domain required for group I intron self-splicing [7].

References