The primary structure of the 5 S RNA binding protein L25 from <i>Escherichia coli</i> ribosomes

Dovgas, N.V.; Markova, L.F.; Mednikova, T.A.; Vinokurov, Leonid M.; Alakhov, Yu.B.; Ovchinnikov, Yu.A.

doi:10.1016/0014-5793(75)80053-6

Cited by 27 publications

(10 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The specific radioactivity of the 3H-labeled proteins was approximately 2500 counts/min per gg; the specific acitivity of 14C-and 32P-labeled 5S RNA ranged from 2 X 103 to 2 X 106 counts/min per gg. Sequence molecular weights for proteins L5, LI8, and L25 are 20 172 (Chen & Ehrke, 1976), 12 770 (Brosius et al, 1975), and 10 912 (Dovgas et al, 1975), respectively; that for 5S RNA was calculated to be 38 853 from its base composition (Brownlee et al, 1967).…”

Section: Methodsmentioning

confidence: 99%

“…Since the circular dichroism of L5, LI 8, and L25 was undetectable from 240 to 305 nm, a mean nucleotide molecular weight of 322 was used for the 5S RNA, whether free or bound, throughout this region. For the calculation of CD spectra from 215 to 240 nm, mean residue weights for L5, L18, L25, L5-5S RNA, L18-5S RNA, L25-5S RNA, and L5, LI 8, L25-5S RNA were taken to be 113, 109, 114, 197, 227, 231, and 162, respectively, on the basis of amino acid and nucleotide composition (Chen & Ehrke, 1976;Brosius et al, 1975;Dovgas et al, 1975;Brownlee et al, 1967).…”

Section: Methodsmentioning

confidence: 99%

“…near 1:1 under optimal conditions (Spierer . The complete primary structures of the three proteins and of the 58 RNA are known (Brosius et al, 1975; Dovgas et al, 1975;Chen & Ehrke, 1976;Brownlee et al, 1967) and nucleotide sequences to which the proteins bind have been described (Gray et al, 1973;Zimmermann & Erdmann, 1978). Interactions involving L5 and L18 have also been found to possess a strongly cooperative character (Feunteun et al, 1975; Spierer that is strikingly reflected in the ability of the ternary L5, L18-5S RNA complex to associate with 238 RNA (Gray et al, 1972;.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Structure and macromolecular interactions of 5S RNA. 2. Parameters for the interaction of ribosomal proteins L5, L18, and L25 with 5S RNA from Escherichia coli

Spierer¹,

Bogdanov²,

Zimmermann³

1978

Biochemistry

View full text Add to dashboard Cite

Association constants (AY) for the binding of 50S ribosomal subunit proteins L5, LI8, and L25 to the 5S ribosomal RNA of Escherichia coli have been determined by a membrane filter assay. Values for AY are 2.3 X 108 M_l for the L18-5S RNA complex, 1.5 X 107 M~' for the L25-5S RNA complex, and 2.3 X 106 M_1 for the L5-5S RNA complex at 25 °C in TMK buffer (50 mM Tris-HCl (pH 7.6)-20 mM MgCH-SOO mM KC1). Although the affinity of L5 increases by approximately one order of magnitude in the presence of L18, estimation of AY was not feasible in the ternary complex. Standard thermodynamic quantities for the

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Structure and macromolecular interactions of 5S RNA. 2. Parameters for the interaction of ribosomal proteins L5, L18, and L25 with 5S RNA from Escherichia coli

Spierer¹,

Bogdanov²,

Zimmermann³

1978

Biochemistry

View full text Add to dashboard Cite

show abstract

“…protein complex [4]. The sequence of the 5-S RNA from a large number of prokaryotes has been determined [5] and the complete amino acid sequences of the ribosomal proteins EL5 [ 6 ] , EL18 [7] and EL25 [8,9] are now known. …”

mentioning

confidence: 99%

The 5‐S RNA · Protein Complex from an Extreme Halophile, Halobacterium cutirubrum

Smith

Yaguchi

Willick

et al. 1978

European Journal of Biochemistry

View full text Add to dashboard Cite

A 5-S RNA . protein complex has been isolated from the 50-S ribosomal subunit of an extreme halophile, Hulobacterium cutirubrum. The 50-S ribosomal subunit from the extreme halophile requires 3.4 M K' and 100 mM Mg" for stability. However, if the high K' concentration is maintained but the Mg2' concentration lowered to 0.3 mM, the 5-S RNA . protein complex is selectively extracted from the subunit. After being purified on an Agarose 0.5-m column the complex had a molecular weight of about 80000 and contained 5-S RNA and two proteins, HL13 and HL19, with molecular weights (by sedimentation equilibrium) of 18 700 and 18000, respectively. No ATPase or GTPase activity could be detected in the 5-S RNA . protein complex. The amino acid composition and electrophoretic mobility on polyacrylamidc gels indicated both proteins were much more acidic than the equivalent from Escherichia coli or Bacillus steurotliermoI)hilus. Partial amino acid sequence data suggest HL13 is homologous to EL18 and HL19 to EL5.The 5-S RNA, a component of the 50-S ribosomal subunit of all prokaryotes, is believed to play a key role in the structure and function of the ribosome. Studies by Erdmann and his co-workers (see [1] for review) have indicated that the 5-S RNA forms part of the aminoacyl-tRNA binding site on the ribosome specifically interacting with the T-Y-C-G sequence in the tRNA through a G-A-A-C nucleotide sequence. The 5-S RNA is also thought to be involved in the translocation step in protein synthesis [2].In Eschericliiu coli, two proteins, ELI8 and EL25, specifically bind to the 5-S RNA [3] while in the therniophile Bacillus stcarotlicrrnc~~~hilus BL5 and BL22 have a similar role [3]. There is also evidence in E. coli that a third protein EL5 is also part of the 5-S RNA . protein complex [4]. The sequence of the 5-S RNA from a large number of prokaryotes has been determined [5] and the complete amino acid sequences of the ribosomal proteins EL5 [ 6 ] , EL18 [7] and EL25 [8,9] are now known.

show abstract

“…The primary structure of this protein was recently determined by Ovchinnikov and his collaborators at our Institute [2]. Starting with the assumption that this protein has a globular structure in water environment we have attempted to determine its tertiary structure proceeding from the primary one.…”

Section: Introductionmentioning

confidence: 99%

Prediction of the three‐dimensional structure for ribosomal protein L25

1975

View full text Add to dashboard Cite

The primary structure of the 5 S RNA binding protein L25 from Escherichia coli ribosomes

Cited by 27 publications

References 5 publications

Structure and macromolecular interactions of 5S RNA. 2. Parameters for the interaction of ribosomal proteins L5, L18, and L25 with 5S RNA from Escherichia coli

Structure and macromolecular interactions of 5S RNA. 2. Parameters for the interaction of ribosomal proteins L5, L18, and L25 with 5S RNA from Escherichia coli

The 5‐S RNA · Protein Complex from an Extreme Halophile, Halobacterium cutirubrum

Prediction of the three‐dimensional structure for ribosomal protein L25

Contact Info

Product

Resources

About