HL35e and HLA: Primary structure of two very basic and cysteine-rich ribosomal proteins from Haloarcula marismortui

Bergmann, Ulrike; Wittmann‐Liebold, Brigitte

doi:10.1016/0167-4781(93)90181-c

Cited by 4 publications

(1 citation statement)

References 27 publications

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“…Of the 56 residues of the rat ribosomal protein S29, 4 are Cys (also 7%). 91 Zinc fingers are present in ribosomal proteins of Archaea, 92,93 Bacteria, 94,95 and Eukaryotes. 96,97 They are also part of aminoacyl-tRNA synthetases (e.g., AlaRS, 98 GluRS, 99 MetRS).…”

Section: Scheme 14 Electrochemistry Of 4fe-4s Clustersmentioning

confidence: 99%

Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa

Youssef-Saliba

Vallée

2021

Synthesis

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Two sulfur containing amino acids are included in the list of the 20 classical protein amino acids. A methionine residue is introduced at the start of the synthesis of all current proteins. Cysteine, thanks to its thiol function, plays an essential role in a very large number of catalytic sites. Here we present what is known about the prebiotic synthesis of these two amino acids and homocysteine, and we discuss their introduction into primitive peptides and more elaborate proteins.

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Section: Scheme 14 Electrochemistry Of 4fe-4s Clustersmentioning

confidence: 99%

Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa

Youssef-Saliba

Vallée

2021

Synthesis

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Cell Cycle, Differentiation and Tissue‐Independent Expression of Ribosomal Protein L37

Bird

1995

European Journal of Biochemistry

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A unique human cDNA (hG1.16) that encodes a mRNA of 450 nucleotides was isolated from a subtractive library derived from HeLa cells. The relative expression level of hG1. 16 during different cellcycle phases was determined by Northern-blot analysis of cells synchronized by double-thymidine block and serum deprivatiodrefeeding. hG1.16 was constitutively expressed during all phases of the cell cycle, including the quiescent phase when even most constitutively expressed genes experience some suppression of expression. The expression level of hG1.16 did not change during terminal differentiation of myoblasts to myotubes, during which cells become permanently post-mitotic. Examination of other tissues revealed that the relative expression level of hG1.16 was constitutive in all embryonic mouse tissues examined, including brain, eye, heart, kidney, liver, lung and skeletal muscle. This was unusual in that expression was not down-modulated during differentiation and did not vary appreciably between tissue types. Analysis by inter-species Northern-blot analysis revealed that hGl. 16 was highly conserved among all vertebrates studied (from fish to humans but not in insects). DNA sequence analysis of hGf.16 revealed a high level of similarity to rat ribosomal protein L37, identifying hG1.16 as a new member of this multigene family. The deduced amino acid sequence of hGf .f 6 was identical to rat ribosomal protein L37 that contained 97 amino acids, many of which are highly positively charged (15 arginine and 14 lysine residues with a predicted M, of 11 065). hG1.16 protein has a single C,-C, zinc-finger-like motif which is also present in rat ribosomal protein L37. Using primers designed from the sequence of hG1.16, unique bovine and rat cDNAs were also isolated by 5'-rapid-amplification of cDNA ends. DNA sequences of bovine and rat G1.16, clones were 92.8 % and 92.2 % similar to human G1 .I 6 while the deduced amino acid sequences derived from bovine and rat cDNAs each differed by a single amino acid from the sequence of hG1.16 and the published rat L37 sequence. Southern-blot analysis revealed that hG1.16 exists in multiple copies in human, rat and mouse genomes. These G1.16 clones encode unique human, rat and bovine members of the ribosomal protein L37 gene family, which are constitutively expressed even during transitions from quiescence to active cell proliferation or terminal differentiation, in all tissues and all vertebrates investigated.

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Cell Cycle, Differentiation and Tissue-Independent Expression of Ribosomal Protein L37

Su¹,

Bird²

1995

Eur J Biochem

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A unique human cDNA (hG1.16) that encodes a mRNA of 450 nucleotides was isolated from a subtractive library derived from HeLa cells. The relative expression level of hG1.16 during different cell‐cycle phases was determined by Northern‐blot analysis of cells synchronized by double‐thymidine block and serum deprivation/refeeding. hG1.16 was constitutively expressed during all phases of the cell cycle, including the quiescent phase when even most constitutively expressed genes experience some suppression of expression. The expression level of hG1.16 did not change during terminal differentiation of myoblasts to myotubes, during which cells become permanently post‐mitotic. Examination of other tissues revealed that the relative expression level of hG1.16 was constitutive in all embryonic mouse tissues examined, including brain, eye, heart, kidney, liver, lung and skeletal muscle. This was unusual in that expression was not down‐modulated during differentiation and did not vary appreciably between tissue types. Analysis by inter‐species Northern‐blot analysis revealed that hG1.16 was highly conserved among all vertebrates studied (from fish to humans but not in insects). DNA sequence analysis of hG1.16 revealed a high level of similarity to rat ribosomal protein L37, identifying hG1.16 as a new member of this multigene family. The deduced amino acid sequence of hG1.16 was identical to rat ribosomal protein L37 that contained 97 amino acids, many of which are highly positively charged (15 arginine and 14 lysine residues with a predicted Mr of 11065). hG1.16 protein has a single C2‐C2 zinc‐finger‐like motif which is also present in rat ribosomal protein L37. Using primers designed from the sequence of hG1.16, unique bovine and rat cDNAs were also isolated by 5′‐rapid‐amplification of cDNA ends. DNA sequences of bovine and rat G1.16, clones were 92.8% and 92.2% similar to human G1.16 while the deduced amino acid sequences derived from bovine and rat cDNAs each differed by a single amino acid from the sequence of hG1.16 and the published rat L37 sequence. Southern‐blot analysis revealed that hG1.16 exists in multiple copies in human, rat and mouse genomes. These G1.16 clones encode unique human, rat and bovine members of the ribosomal protein L37 gene family, which are constitutively expressed even during transitions from quiescence to active cell proliferation or terminal differentiation, in all tissues and all vertebrates investigated.

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HL35e and HLA: Primary structure of two very basic and cysteine-rich ribosomal proteins from Haloarcula marismortui

Cited by 4 publications

References 27 publications

Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa

Sulfur Amino Acids: From Prebiotic Chemistry to Biology and Vice Versa

Cell Cycle, Differentiation and Tissue‐Independent Expression of Ribosomal Protein L37

Cell Cycle, Differentiation and Tissue-Independent Expression of Ribosomal Protein L37

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