The primary structure of protein L15 located at the peptidyl‐transferase center of <i>Escherichia coli</i> ribosomes

Giorginis, S.; Chen, Robert

doi:10.1016/0014-5793(77)80722-9

Cited by 14 publications

(4 citation statements)

References 15 publications

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“…The DNA sequence has also confirmed and refined the amino acid sequences of the ten r-proteins of the spc operon. The amino acid sequences as deduced from the DNA sequence for L24, S8, L18, S5, L30 and L15 show complete agreement with published amino acid sequences (15,18,20,21,22,23). However, discrepancies have been found for L14, L5, S14 and L6 (14,16,17,19).…”

Section: Resultssupporting

confidence: 74%

Thespcrtbosomal protein operon ofEschenchia coli:sequence and cotranscriptlon of the rlbosomal protein genes and a protein export gene

Cerretti¹,

Dean²,

Davis³

et al. 1983

Nucl Acids Res

258

121

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The genes encoding the 52 ribosomal proteins (r-proteins) of Escherichia coli are organized into approximately 19 operons scattered throughout the chromosome. One of these, the spc operon, contains the genes for ten ribosomal proteins: L14, L24, L5, S14, S8, L6, L18, S5, L30 and L15 (rp1N, rp1X, rp1E, rpsN, rpsH, rp1F, rp1R, rpsE, rpmD, and rp1O). We now report the entire 5.9 kb nucleotide sequence of the spc operon. DNA sequence analysis has confirmed the genetic organization and refined the amino acid sequence of the ten r-proteins in this operon. It has also revealed the presence of two open reading frames past the last known gene (L15) of the spc operon. One of these corresponds to a gene (pr1A or secY) which recently has been shown by others to be involved in protein export. In addition, S1 mapping experiments indicate that a significant proportion of transcription initiated from the spc operon continues not only into the two putative genes, but also without termination into the downstream alpha r-protein operon.

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Section: Resultssupporting

confidence: 74%

Thespcrtbosomal protein operon ofEschenchia coli:sequence and cotranscriptlon of the rlbosomal protein genes and a protein export gene

Cerretti¹,

Dean²,

Davis³

et al. 1983

Nucl Acids Res

258

121

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“…. PV Amino acid sequence comparisons of CL15 from Arabidopsis thaliana (AtCL15), Pisum sativum (PsCL15) and Escherichia coli (EEL15)[ 17]. Position 1 corresponds to the N-terminal methionine of the A. thaliana protein derived from the eDNA and genomic sequences.…”

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confidence: 99%

Characterization of rps17, rpl9 and rpl15: three nucleus-encoded plastid ribosomal protein genes

et al. 1992

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Approximately two-thirds of the 55 to 60 plastid ribosomal proteins are encoded in the nucleus. Since the protein products of each of these genes are needed in equal amounts for ribosome assembly, their expression may be coordinately regulated by common mechanisms. To begin to understand how the expression of these genes is regulated, we have isolated cDNA and genomic clones for three plastid ribosomal protein genes from an Arabidopsis thaliana library. The genes rps17, rpl9 and rpl15, encoding plastid ribosomal proteins CS17, CL9 and CL15, respectively, are located in the nuclear genome and Southern blot data suggest that each is a single copy gene in A. thaliana. Northern blot data show that transcripts from rps17, rpl9 and rpl15 are much more abundant in leaves and stems than they are in roots. The nucleotide sequences of each of these three genes were determined and their transcriptional initiation sites identified. rps17 transcripts have multiple 5' ends suggesting that they are initiated at multiple sites or are post-transcriptionally processed at their 5' end. rpl9 and rpl15 apparently have unique transcriptional initiation sites but are post-transcriptionally processed to remove six and three introns, respectively, from their primary transcripts. We have examined the genomic sequences for motifs that may be important for the proper expression of these genes. A 7 bp sequence motif, whose consensus is 5'-AGGCCCA-3', flanked by AT-rich regions was identified between 38 and 73 nucleotides upstream of the rps17, rpl9 and rpl15 transcriptional initiation sites.

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“…The complete amino acid sequences of the proteins were determined by analyses of the overlapping peptides produced with one of the following enzymes: trypsin (treated with N - Fig. 1 [27] and L30 / X I / , a/?d rat ( L 1 9 /1.3/,. Amino acid residues identical to those in halobacterial proteins are enclosed i n boxcs.…”

Section: Sequence Determinationmentioning

confidence: 99%

“…Fig. 1 D shows the alignment of the sequences of L9 and the homologous proteins; yeast L29 (251, B. stearothermophilus L15 [26] and E. coli L15 [27]. Intercstingly, there are relatively long gaps in the alignment between H .…”

Section: Comparison Of' [He Amino Acid Sequencesmentioning

confidence: 99%

Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins

Hatakeyama¹,

KAUFMANN²,

SCHROETER³

et al. 1989

European Journal of Biochemistry

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RESULTS isolation of the proteinsThe proteins extracted from 50s ribosomal subunits of H . rnarismortui were separated by DEAE-cellulose chromatography. Fig. S1 shows the two-dimensional gel electrophoretic pattern of 50s ribosomal proteins and Fig. S2 indicates their elution positions from the DEAE-cellulose column. Appropriate fractions were pooled then further separated by gel filtration or revcrse-phasc HPLC, as described in Materials and Methods. Purified proteins were subjected to sequence analysis.Protein L21i22, which eluted as a single peak on reverse-phase HPLC, was subjected to sequence analysis without further purification. This protein also showed a single N-terminal sequence. Sequence determinationThe complete amino acid sequcnces and the sequencing strategy of H. rnarisrnortui ribosomal proteins L9, L20, L21122, L24 and L32 are given in Fig.S3. The results were obtained by sequencing of overlapping peptides produced using trypsin, chymotrypsin. S. aureus protease, thermolysin and lysyl endopeptidase. In the case of protein H. rnarisrnortui L20, we had difficulties in scquencing the middle region (positions 77-83) of the protein manually. This problem was solved with the aid of the gas-phase sequenator which yielded the sequence of the tryptic peptide TS up to position 94. The cleavage between peptides T5 and T6 of protcin L20, i.e. at the carboxyl side of phenylalanine, may have resulted from an intrinsic chymotryptic activity of thc trypsin preparation uscd in this case.The N-terminal sequcnces of H . marismortui L9 and L20 are in gcneral agreement with those of proteins L7 and L16 whose N-termini were sequenced after blotting from two-dimensional eelctrophoresis gels by Walsh et al. [29], although there are discrcpancics at three positions between the sequences of H . marismortui L9 and L7 in [29]; positions 1, 30 and 31 of protein L7 were determined to be aspartic acid, asparagine and arginine, respectively.19. Dayhoff, M. 0. (1978)

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The primary structure of protein L15 located at the peptidyl‐transferase center of Escherichia coli ribosomes

Cited by 14 publications

References 15 publications

Thespcrtbosomal protein operon ofEschenchia coli:sequence and cotranscriptlon of the rlbosomal protein genes and a protein export gene

Thespcrtbosomal protein operon ofEschenchia coli:sequence and cotranscriptlon of the rlbosomal protein genes and a protein export gene

Characterization of rps17, rpl9 and rpl15: three nucleus-encoded plastid ribosomal protein genes

Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins

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