1974
DOI: 10.1016/0014-5793(74)80983-x
|View full text |Cite
|
Sign up to set email alerts
|

An acidic, alanine‐rich 50 S ribosomal protein from Halobacterium cutirubrum: Amino acid sequence homology with Escherichia coli proteins L7 and L12

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

1
6
0
1

Year Published

1975
1975
1987
1987

Publication Types

Select...
4
3

Relationship

0
7

Authors

Journals

citations
Cited by 36 publications
(8 citation statements)
references
References 10 publications
1
6
0
1
Order By: Relevance
“…Thus, a similar type protein(s) has also been found in Halobacteria cutirubrum (43)(44)(45), Bacillus stearothermophilus (46,47), yeast (48), rat liver (49), chicken liver (50), and Arternia salina (51). The protein from B. stearothermophilus (A2) can substitute for E. coli L7/L12 on the E. coli ribosome and support protein synthesis [Table 3 (52)].…”
Section: L12-like Proteins From Other Speciesmentioning
confidence: 91%
See 1 more Smart Citation
“…Thus, a similar type protein(s) has also been found in Halobacteria cutirubrum (43)(44)(45), Bacillus stearothermophilus (46,47), yeast (48), rat liver (49), chicken liver (50), and Arternia salina (51). The protein from B. stearothermophilus (A2) can substitute for E. coli L7/L12 on the E. coli ribosome and support protein synthesis [Table 3 (52)].…”
Section: L12-like Proteins From Other Speciesmentioning
confidence: 91%
“…There appears to be little homology between E. coli and A. salina except for an alanine rich area in both proteins (54). Oda et al (44) have pointed out that although the respective proteins from E. coli and H. cutirubrum show no immunological or biological cross-reactivity, when the first amino acid of HL20 is aligned with residue 35 ofE. coli L7/LI2, then 13 of the first 30 amino acids of HL20 are identical to the E. coli L7/L12 amino acids.…”
mentioning
confidence: 97%
“…However, comparisons with eubacterial and eucaryotic ribosomes are hampered by the complexity of the ribosome and incomplete sets of data on ribosomal proteins from other kingdoms. Although immunological and protein sequence data have identified a number of homologies with eubacterial and eucaryotic proteins, these studies are far from complete (9,241,308,310,348,398,401,402,531). The early observation that ribosomal proteins of archaebacteria are unusually acidic is well correlated with the intracytoplasmic concentrations of ions in halobacteria and some methanogens and is probably not of major phylogenetic significance (196).…”
Section: Ribosomal Proteinsmentioning
confidence: 99%
“…The early observation that ribosomal proteins of archaebacteria are unusually acidic is well correlated with the intracytoplasmic concentrations of ions in halobacteria and some methanogens and is probably not of major phylogenetic significance (196). The archaebacterial ribosomal "A" proteins, whose complete sequence is known, has substantial homology to the eucaryotic "A" protein and much less homology to the eubacterial equivalent, L12 (308,309,348). Similarly, the archaebacterial 5S RNA-binding proteins have more sequence homology to the eucaryotic than to the eubacterial proteins (9,241).…”
Section: Ribosomal Proteinsmentioning
confidence: 99%
“…wt acidic protein, which is involved in elongation factor-dependent GTP hydrolysis [ 1 ]. A similar protein has been detected in the ribosomes of a number of eucaryotic organisms [2], and primary structure studies of the proteins of procaryotes and eucaryotes have been initiated [3][4][5]. Recently, it was found that the aminoterminal region of L7/L12-protein from Artemia salina and Saccharomyces cerevisiae shows a sequence homology with the corresponding region of the protein from Halobacterium cutirubrum [6].…”
Section: Introductionmentioning
confidence: 99%