Escherichia coli initiation factor 3 protein binding to 30S ribosomal subunits alters the accessibility of nucleotides within the conserved central region of 16S rRNA

Biochemistry ◽  
1989 ◽  
Vol 28 (19) ◽  
pp. 7505-7510 ◽  
Author(s):  
Parimi Muralikrishna ◽  
Eric Wickstrom
Keyword(s):  
Escherichia Coli ◽  
16S Rrna ◽  
Protein Binding ◽  
Central Region ◽  
Initiation Factor ◽  
Ribosomal Subunits

scholarly journals Photochemical cross-linking of initiation factor-3 to Escherichia coli 30 S ribosomal subunits.

1980 ◽  
Vol 255 (21) ◽  
pp. 10526-10531
Author(s):  
L.A. MacKeen ◽  
L. Kahan ◽  
A.J. Wahba ◽  
I. Schwartz
Keyword(s):  
Escherichia Coli ◽  
Initiation Factor ◽  
Cross Linking ◽  
Ribosomal Subunits

scholarly journals Functional investigation of residue G791 of Escherichia coli 16S rRNA: implication of initiation factor 1 in the restoration of P-site function

2010 ◽  
Vol 313 (2) ◽  
pp. 141-147
Author(s):  
Woo-Seok Song ◽  
Sang-Mi Ryou ◽  
Hong-Man Kim ◽  
Che Ok Jeon ◽  
Jong-Myung Kim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
16S Rrna ◽  
Initiation Factor ◽  
Site Function ◽  
Functional Investigation

scholarly journals Novel Plasmid-Mediated 16S rRNA m1A1408 Methyltransferase, NpmA, Found in a Clinically Isolated Escherichia coli Strain Resistant to Structurally Diverse Aminoglycosides

2007 ◽  
Vol 51 (12) ◽  
pp. 4401-4409 ◽  
Author(s):  
Jun-ichi Wachino ◽  
Keigo Shibayama ◽  
Hiroshi Kurokawa ◽  
Kouji Kimura ◽  
Kunikazu Yamane ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
16S Rrna ◽  
Recombinant Plasmid ◽  
Coli Strain ◽  
Methyltransferase Activity ◽  
Ribosomal Subunits ◽  
E Coli ◽  
Rrna Molecule ◽  
A Site

ABSTRACT We have isolated a multiple-aminoglycoside-resistant Escherichia coli strain, strain ARS3, and have been the first to identify a novel plasmid-mediated 16S rRNA methyltransferase, NpmA. This new enzyme shared a relatively low level of identity (30%) to the chromosomally encoded 16S rRNA methyltransferase (KamA) of Streptomyces tenjimariensis, an actinomycete aminoglycoside producer. The introduction of a recombinant plasmid carrying npmA could confer on E. coli consistent resistance to both 4,6-disubstituted 2-deoxystreptamines, such as amikacin and gentamicin, and 4,5-disubstituted 2-deoxystreptamines, including neomycin and ribostamycin. The histidine-tagged NpmA elucidated methyltransferase activity against 30S ribosomal subunits but not against 50S subunits and the naked 16S rRNA molecule in vitro. We further confirmed that NpmA is an adenine N-1 methyltransferase specific for the A1408 position at the A site of 16S rRNA. Drug footprinting data indicated that binding of aminoglycosides to the target site was apparently interrupted by methylation at the A1408 position. These observations demonstrate that NpmA is a novel plasmid-mediated 16S rRNA methyltransferase that provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N-1 methylation at position A1408.

Binding of initiation factor 2 and initiator tRNA to the Escherichia coli 30S ribosomal subunit induces allosteric transitions in 16S rRNA

Biochemistry ◽  
1990 ◽  
Vol 29 (35) ◽  
pp. 8144-8151 ◽  
Author(s):  
Hiroshi Wakao ◽  
Pascale Romby ◽  
Soumaya Laalami ◽  
Jean Pierre Ebel ◽  
Chantal Ehresmann ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
16S Rrna ◽  
Ribosomal Subunit ◽  
Initiation Factor ◽  
Initiator Trna ◽  
Initiation Factor 2 ◽  
Allosteric Transitions

Crosslinking of Escherichia coli initiation factor IF-3 to the RNA moiety of the 30S ribosomal subunits

Biochemistry ◽  
1977 ◽  
Vol 16 (26) ◽  
pp. 5681-5686 ◽  
Author(s):  
Cynthia L. Pon ◽  
Richard Brimacombe ◽  
Claudio Gualerzi
Keyword(s):  
Escherichia Coli ◽  
Initiation Factor ◽  
Ribosomal Subunits
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