Disease relevance of mreB

• Inactivation of the mreB gene was incompatible with viability, and thus mreB represents a Streptomyces cell division gene that is essential for survival [1].
• However, in E. coli, mreB was inferred not to be essential [2].
• A gene with substantial sequence similarity to the mreB morphogene of Bacillus subtilis has been identified at 302 degrees on the chromosomal map by A [3].
• Cloning of a gene from Bacillus cereus with homology to the mreB gene from Escherichia coli [4].
• Extended phenotype of an mreB-like mutant in Azospirillum brasilense [5].

High impact information on mreB

• Although the mreB null mutant showed a drastic change in cell shape, its growth rate, cell division and the filament length were unaltered [6].
• Although the mre determinants are not required for viability in E. coli, the mreB determinant is an essential gene in B. subtilis [7].
• In E. coli, the yhdA and mreB genes are adjacent to each other on the chromosome [8].
• The B. subtilis mreB, mreC, and mreD genes are the site of a conditional mutation (rodB1) that causes the production of aberrantly shaped cells under restrictive conditions [9].
• The deduced 557-amino-acid sequence of the large-CRP gene (envB) contains 37 cysteine residues and a single putative signal peptidase I cleavage site [10].

Biological context of mreB

• Introduction of a frame-shift mutation in the mreB gene resulted in a significant decrease in the amount of polycistronic mreBCD mRNA but not in that of monocistronic mreB mRNA, suggesting that an attenuation-like regulation was involved in this transcriptional control [11].
• Based on the sequence, it is suggested that the three mre genes (encoding the murein pathway), mreB, mreC and mreD, and these two ORFs possibly form an operon [12].
• The mreB protein and some of these three proteins may function together in determination of cell shape [13].
• An open reading frame that may code for a protein with an Mr of about 37,000 on sodium dodecyl sulfate-polyacrylamide gels was found and was correlated with the mreB gene [13].
• Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells [13].

Anatomical context of mreB

• Electron microscopy shows that the cytoplasmic membrane of growing mon and envC cells is dissolved by detergents, and that the cytoplasm dissociates into two parts of unequal density [14].

Associations of mreB with chemical compounds

• The delta mre-678 mutant cells required three genes, the previously reported mreB gene and the two new genes, to restore the normal rod shape of the cells and normal sensitivity of growth to mecillinam [15].

Other interactions of mreB

• The mreC gene is preceded by the mreB gene and by a 65-base-pair spacing sequence containing a palindrome sequence and a possible Shine-Dalgarno sequence [15].
• N-terminal amino acid sequencing of the hybrid mreB-lacZ protein confirmed the production by mreB of a protein of 347 amino acid residues with a molecular weight of 36,958 [13].

References