Structure primaire de la paracaseine κ bovine

Brignon, Ghislaine; Mercier, Jean‐Claude; Ribadeau‐Dumas, B.; Das, Bhupesh C.

doi:10.1016/0014-5793(72)80646-x

Cited by 36 publications

(10 citation statements)

References 15 publications

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“…In the bovine caseins it has been shown that the phosphorylated serine residues are all followed by an acidic amino acid two residues downstream [21] and that the phosphorylated residues are clustered in a region rich in acidic amino acids [3]. The same could hold true for mouse F casein.…”

Section: Gac Atc Att Tct Cag Caamentioning

confidence: 93%

“…3) the aminoterminal methionine is followed in all but one case (ovine CI lactalbumin) by either a lysine or an arginine, which also might be important in stabilizing the nascent-chain -membrane-receptor complex through additional ionic bonds [20]. The amino acid sequences of all bovine caseins have been determined [2,3]. Mature mouse E casein and mature bovine c(,2 casein show partial homology in their N-terminal region (Fig.4A).…”

Section: Gac Atc Att Tct Cag Caamentioning

confidence: 99%

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Nucleotide Sequence of Cloned cDNA Coding for Mouse ɛ Casein

Hennighausen

Steudle

Sippel

1982

European Journal of Biochemistry

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We isolated cDNA clones, which correspond to the mRNA coding for the smallest of the seven mouse caseins. From the nucleotide sequence of the cDNA we deduced the amino acid sequence of the protein, which we named E casein. Mouse E casein and cow M,Z casein show amino acid sequence homologies in the N-terminal region of the mature protein. The signal peptide of mouse E casein shows in length and sequence remarkable homology to the signal peptides of the calcium-precipitable caseins of other species. In accordance with this group of caseins mouse E casein contains in the sequence -Ser-Ser-Glu-Glu-a site for potential multiple phosphorylation.Caseins are the major secretory proteins synthesized in the lactating mammary gland [1,2]. They are mostly phosphoproteins, which are stored and excreted in the milk as stable aggregates called micelles. In bovine milk these complexes depend on hydrophobic interactions between non-polar segments of aSl, CI,Z and p casein [2]. The negatively charged residues of the caseins are concentrated in a small portion of the polypeptide chain and they interact with calcium and x casein. x casein stabilizes the micellar structure by protecting the aggregated caseins against uncontrolled precipitation.The purification and detailed structural analysis have been confined to the bovine [l -61 and ovine [7,8] caseins. We have recently characterized the mRNAs and cloned the respective cDNAs for all eight major mouse milk proteins [9]. The present communication reports the complete primary structure of mouse E casein as predicted from the nucleotide sequence of cloned cDNA. Mouse E casein and bovine a ,~ casein share common sequences in their N-terminal region, which include the potential serine phosphorylation site -Ser-Ser-Glu-Glu-. Knowledge of the structural features of caseins are important to understand the micellar structure of protein aggregates in the milk. MATERIALS AND METHODS MaterialsRadiochemicals were obtained from Amersham. Restriction endonucleases, Escherichia coli DNA polymerase I (large fragment) and deoxynucleotide triphosphates were from Boehringer. Dimethylsulfate, hydrazinium hydroxide and piperidine were supplied by Merck. MethodsThe mRNA of the smallest mouse casein has been isolated, characterized and cloned in our laboratory as described previously [9]. Recombinant plasmid DNA was isolated according to Birnboim and Doly [lo]. After digestion of the plasmid DNA with restriction endonucleases, outlined in Fig. 1, the DNA fragments were labelled at one end directly in the restriction buffer. 3' intruding ends were labelled for 10 min at 15 "C in a 50-pl assay containing 4 U E. coli DNA polymerase I (large fragment) and a twofold molar excess of the appropriate [ M -~~P I~N T P .The P.vtI site was labelled for 45 min at 25 'C in an assay containing 1 mM dTTP, 4 U E. coli DNA polymerase I (large fragment) and a fourfold molar excess of [cI-~'P]~CTP over PstI sites. Under those conditions it was possible to label the 5'-positioned dCMP of the PstI restriction site by limite...

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Section: Gac Atc Att Tct Cag Caamentioning

confidence: 93%

Section: Gac Atc Att Tct Cag Caamentioning

confidence: 99%

Nucleotide Sequence of Cloned cDNA Coding for Mouse ɛ Casein

Hennighausen

Steudle

Sippel

1982

European Journal of Biochemistry

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“…Known phosphoserine residues in the bovine sequence [24] are indicated (by P). Potential phosphoserine residues in the bovine and guinea-pig sequences are indicated by asterisks.…”

Section: Comparison Of Bovine Usz Casein With the Deduced Guinea-pig mentioning

confidence: 99%

Guinea‐pig casein A cDNA

Hall

Laird

Pascall

et al. 1984

European Journal of Biochemistry

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The nucleotide sequence (1036 bases) of guinea-pig casein A mRNA has been determined. Two cDNA recombinant plasmids contained a total of 993 base pairs, including part of the 5' noncoding region, and the complete coding and 3' noncoding region. The remaining 5' noncoding sequence was obtained by primer extension.The deduced 223-amino-acid-coding sequence of guinea-pig pre-casein A exhibited 30 % homology with bovine uS2 casein, the most striking similarities being in the locations of potential phosphorylation sites.During lactation, the expression of the milk protein genes of the epithelial cells of the mammary gland is modulated by a combination of peptide and steroid hormones [I]. An attractive feature of this system is that differential regulation of the a-lactalbumin and casein genes is apparent during the onset of lactation [2 -41, making it a particularly suitable system for studying the hormonal control of a family of genes.In the course of our studies using the lactating guinea-pig mammary gland as a model system, we have cloned and characterised cDNA copies of the three major guinea-pig casein mRNAs and cr-lactalbumin mRNA [5]. We have recently reported the sequence of the latter [6]. We now report the complete nucleotide sequence of one of the casein cDNAs, that encoding guinea-pig casein A (using our previous nomenclature based on the relative mobility of the protein on polyacrylamide gels [7]). This was a necessary prerequisite for our current studies on the genomic organisation, expression and hormonal regulation of the milk protein genes. Examination of the amino acid sequence of this casein, deduced from the nucleotide sequence, reveals significant homology with bovine a;, casein. This is most apparent in terms of the locations of potential phosphorylation sites and sequences of the signal peptide, implicating a conservation of these functionally important domains. MATERIALS AND METHODS Muter iulsRestriction endonucleases BstNI, Fnu4HI and RsaI were purchased from Bio-Labs through CP Labs Ltd (Bishop's Stortford, Herts, UK); all other restriction enzymes, T4 DNA polymerase and T4 polynucleotide kinase were from Bethesda Research Labs (Cambridge UK). AMV reverse transcriptase (batch G-91180) was provided by. Dr. J. W. Beard (Life Sciences Inc., St Petersburg, FL, USA). Recombinant plasmidsThe construction and characterisation of pgpN33, a recombinant plasmid containing a cDNA copy of guinea-pig casein A mRNA inserted into the EcoRI site of pAT153 using homopolymeric dA . dT tails, has been described previously [5]. A second recombinant pgpKG8, showing extensive overlap with the inserted sequence of pgpN33 but possessing an additional sequence at one end, was isolated from a similar library obtained by insertion of lactating guinea-pig mammary gland double-stranded cDNA, prepared as described by Land et al.[S], into the PstI site of pAT153 using dG . dC homopolymer tails. Chemical DNA sequencing of recombinant plasmidsProcedures for the preparation of restriction fragments, 5' and 3' end labelling, ...

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“…The K-casein molecules consist of two parts separated by the chymosin-sensitive bond (Jolles, 1966;Delfour et al, 1965; see also below): para-K-casein (NH2-terminal moiety, residues 1-105) and K-caseinoglycopeptide (COOH-terminal moiety, residues 106-169 for cow and 106-171 for sheep K-caseins). The primary structures were previously described by Brignon et al (1972) and Jolles et al (1972) for cow para-Kcasein, Mercier et al (1972) andJolles et al (1973) for cow K-caseinoglycopeptide and by Jolles et al (1974) for sheep K-casein (Fig.. 1). We wish to discuss the secondary structures of both K-caseins and of some of their biologically important sites (see below).…”

Section: Resultsmentioning

confidence: 97%

Prediction of the conformation of the cow and sheep kappa-caseins

Loucheux‐Lefebvre¹,

Aubert²,

Jollès³

1978

Biophysical Journal

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The secondary structures of cow and sheep kappa-caseins were established according to the predictive rules of Chou and Fasman. The diagrams derived from this treatment allowed us to study the chymosin sensitive bond (milk-clotting process), as well as the glycosylation and phosphorylation sites, found to be situated in beta-turns. Despite a high variability between the primary structures of the COOH-terminal part (caseinoglycopeptide) of cow, sheep, and also other caseins, the secondary structures of the biologically important sites were found to be conserved.

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Structure primaire de la paracaseine κ bovine

Abstract: The complete amino acid sequence of bovine para-rcasein is given.

Cited by 36 publications

References 15 publications

Nucleotide Sequence of Cloned cDNA Coding for Mouse ɛ Casein

Nucleotide Sequence of Cloned cDNA Coding for Mouse ɛ Casein

Guinea‐pig casein A cDNA

Prediction of the conformation of the cow and sheep kappa-caseins

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