Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli

Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein component for two essential cellular processes, RNA degradation and transfer-RNA (tRNA) maturation. The first crystal structure of RnpA from the pathogenic bacterial species, S. aureus, is reported at 2.0 Å resolution. The structure presented maintains key similarities with previously reported RnpA structures from bacteria and archaea, including the highly conserved RNR-box region and aromatic residues in the precursor-tRNA 5′-leader-binding domain. This structure will be instrumental in the pursuit of structure-based designed inhibitors targeting RnpA-mediated RNA processing as a novel therapeutic approach for treating S. aureus infections.

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Synthesis of a wheat storage protein subunit in Escherichia coli using novel expression vectors

Gene ◽

10.1016/0378-1119(85)90168-4 ◽

1985 ◽

Vol 35 (1-2) ◽

pp. 159-167 ◽

Cited By ~ 11

Author(s):

D. Bartels ◽

R.D. Thompson ◽

S. Rothstein

Keyword(s):

Escherichia Coli ◽

Storage Protein ◽

Expression Vectors ◽

Protein Subunit ◽

Wheat Storage Protein

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Site-directed mutagenesis of M1 RNA, the RNA subunit of Escherichia coli ribonuclease P

Journal of Molecular Biology ◽

10.1016/0022-2836(86)90253-6 ◽

1986 ◽

Vol 191 (2) ◽

pp. 163-175 ◽

Cited By ~ 19

Author(s):

Nathan P. Lawrence ◽

Sidney Altman

Keyword(s):

Escherichia Coli ◽

Site Directed Mutagenesis ◽

Ribonuclease P ◽

Directed Mutagenesis ◽

M1 Rna

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Substitution of a Highly Conserved Histidine in the Escherichia coli Heat Shock Transcription Factor, σ32, Affects Promoter Utilization In Vitro and Leads to Overexpression of the Biofilm-Associated Flu Protein In Vivo

Journal of Bacteriology ◽

10.1128/jb.01197-07 ◽

2007 ◽

Vol 189 (23) ◽

pp. 8430-8436 ◽

Cited By ~ 2

Author(s):

Olga V. Kourennaia ◽

Pieter L. deHaseth

Keyword(s):

Escherichia Coli ◽

Heat Shock ◽

Rna Polymerase ◽

Sigma Factor ◽

Stable Complex ◽

Tryptophan Residue ◽

Specific Sequence ◽

Bacterial Rna

ABSTRACT The heat shock sigma factor (σ32 in Escherichia coli) directs the bacterial RNA polymerase to promoters of a specific sequence to form a stable complex, competent to initiate transcription of genes whose products mitigate the effects of exposure of the cell to high temperatures. The histidine at position 107 of σ32 is at the homologous position of a tryptophan residue at position 433 of the main sigma factor of E. coli, σ70. This tryptophan is essential for the strand separation step leading to the formation of the initiation-competent RNA polymerase-promoter complex. The heat shock sigma factors of all gammaproteobacteria sequenced have a histidine at this position, while in the alpha- and deltaproteobacteria, it is a tryptophan. In vitro the alanine-for-histidine substitution at position 107 (H107A) destabilizes complexes between the GroE promoter and RNA polymerase containing σ32, implying that H107 plays a role in formation or maintenance of the strand-separated complex. In vivo, the H107A substitution in σ32 impedes recovery from heat shock (exposure to 42°C), and it also leads to overexpression at lower temperatures (30°C) of the Flu protein, which is associated with biofilm formation.

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