Comparison of ribosomal RNA-binding protein “L2” isolated from different bacterial species

Tischendorf, Gilbert; Geisser, M.; Stöffler, Georg

doi:10.1007/bf00333662

Cited by 21 publications

(2 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, preincubation with TP50 lacking protein BL2 had no effect on dimer formation. For this latter experiment, TP50 has been extracted from 50 S subunits with 2 M LiCI/4 M urea, since it has previously been shown that under these conditions protein BL2 remains bound to the 23 S rRNA [8]. Consequently, the protein mixture of TP50, lacks protein BL2 quantitatively as judged by SDSpolyacrylamide gel electrophoresis and immunoblotting (fig.…”

Section: Characterization Of the Antibodymentioning

confidence: 99%

Three‐dimensional location of ribosomal protein BL2 from Bacillus stearothermophilus, a key component of the peptidyl transferase center

Hackl¹,

Stöffler‐Meilicke²,

Stöffler³

1988

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Protein BL2 from Bacillus stearothermophilus has been localized by immunoelectron microscopy on the interface side of the 50 S subunit, beneath the angle formed between the central protuberance and the L1 protuberance. The immunoelectron microscopic data suggest that the interface region of the 50 S particle is not as flat as most of the proposed three-dimensional models suggest, but instead there is a significant concavity. Since several studies demonstrated that BL2 is implicated in peptidyl transferase activity or at least located close to the peptidyl transferase center, the location of protein BL2 also provides information as to the location of this important functional domain.

show abstract

Section: Characterization Of the Antibodymentioning

confidence: 99%

Three‐dimensional location of ribosomal protein BL2 from Bacillus stearothermophilus, a key component of the peptidyl transferase center

Hackl¹,

Stöffler‐Meilicke²,

Stöffler³

1988

FEBS Letters

Self Cite

View full text Add to dashboard Cite

show abstract

“…to the peptidyltransferase active center (for review, see Cantor et al, 1974). One of these, L2, is probably homologous to the B. stearothermophilus protein B-L3, since (1) both have direct binding sites on 23S RNA (Stoffler et al, 1971); (2) they have similar molecular weights and polyacrylamide gel electrophoretic mobilities; and (3) B-L3 crossreacts immunologically with E. coli L2, but not with any of the other E. coli ribosomal proteins (Tischendorf et al, 1973). In view of the one-for-one functional homology between the 30S ribosomal proteins of E. coli and B. stearothermophilus which has been demonstrated by Higo et al (1973) it is reasonable to assume that the structural homology between the 50S proteins B-L3 and L2 reflects a functional homology as well.…”

mentioning

confidence: 99%

Evidence of the involvement of a 50S ribosomal protein in several active sites

Fahnestock¹

1975

Biochemistry

View full text Add to dashboard Cite

The functional role of the Bacillus stearothermophilus 50S ribosomal protein B-L3 (probably homologous to the Escherichia coli protein L2) was examined by chemical modification. The complex [B-L3-23S RNA] was photooxidized in the presence of rose bengal and the modified protein incorporated by reconstitution into 50S ribosomal subunits containing all other unmodified components. Particles containing photooxidized B-L3 are defective in several functional assays, including (1) poly(U)-directed poly(Phe) synthesis, (2) peptidyltransferase activity, (3) ability to associate with a [30S-poly(U)-Phe-tRNA] complex, and (4) binding of elongation factor G and GTP. The rates of loss of the partial functional activities during photooxidation of B-L3 indicate that at least two independent inactivating events are occurring, a faster one, involving oxidation of one or more histidine residues, affecting peptidyltransferase and subunit association activities and a slower one affecting EF-G binding. Therefore the protein B-L3 has one or more histidine residues which are essential for peptidyltransferase and subunit association, and another residue which is essential for EF-G-GTP binding. B-L3 may be the ribosomal peptidyltransferase protein, or a part of the active site, and may contribute functional groups to the other active sites as well.

show abstract

Immunological and electrophoretical comparison of ribosomal proteins from eight species belonging to Enterobacteriaceae

et al. 1973

View full text Add to dashboard Cite

Comparison of ribosomal RNA-binding protein “L2” isolated from different bacterial species

Cited by 21 publications

References 22 publications

Three‐dimensional location of ribosomal protein BL2 from Bacillus stearothermophilus, a key component of the peptidyl transferase center

Three‐dimensional location of ribosomal protein BL2 from Bacillus stearothermophilus, a key component of the peptidyl transferase center

Evidence of the involvement of a 50S ribosomal protein in several active sites

Immunological and electrophoretical comparison of ribosomal proteins from eight species belonging to Enterobacteriaceae

Contact Info

Product

Resources

About