Cloning and nucleotide sequence of the bovine β-lactoglobulin gene

Jamieson, Andrew C.; Vandeyar, Mark A.; Kang, Yuna; Kinsella, John E.; Batt, Carl A.

doi:10.1016/0378-1119(87)90367-2

Cited by 34 publications

(14 citation statements)

References 14 publications

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“…Thus, we would expect to find some evidence for alternative splicing here. The sequence reported for a bovine jB-lactoglobulin cDNA appears to support this; it is very similar to the ovine sequence (44), with the important exception that it lacks the 25-nt sequence homologous to a2-PEG beyond the termination codon. The full sequence of the most downstream 5' splice site in a2-PEG is unknown, but it seems unlikely from inspection of the f3-lactoglobulin genomic sequence that the corresponding GT would act as a 5' splice site even at the level found in a2-PEG (1 in 34 cDNA clones) (Fig.…”

Section: Discussionmentioning

confidence: 61%

Multiple forms of mRNA encoding human pregnancy-associated endometrial alpha 2-globulin, a beta-lactoglobulin homologue.

Garde

Bell

Eperon

1991

Proc. Natl. Acad. Sci. U.S.A.

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Human pregnancy-associated endometrial a2-globulin (a2-PEG) is the major secretory protein product of the endometrium during embryo implantation and the first few weeks of pregnancy. It is a homologue of 8-lactoglobulin, a retinol binding protein, but unlike ig-lactoglobulin it is not found in the mammary gland. The cloning and sequencing of 34 a2-PEG clones has revealed several minor variant forms indicative of alternatively spliced a2-PEG pre-mRNA. These minor forms have also been detected amongs uncloned cDNA after PCR ampfication. Some of these mRNAs would give rise to forms of a2-PEG protein lacking internal sequences, whereas others affect the mRNA sequences on the 3' boundary of the presumed termination codon. Sequences within the cDNA clones are consistent with the existence of splice sites, and together with similarities found between a2-PEG cDNA and ,8-lactoglobulin gene sequences there is good evidence in support of an unusual scheme for the alternative splicing of a2-PEG pre-mRNA involving both alternative 5' splice sites and alternative 3' splice sites. This scheme suggests that the a2-PEG and .3-lactoglobulin genes share a similar structure in at least two regions, and it is likely that 13-lactoglobulin pre-mRNA would show a similar pattern of alternative splicing for one of these regions.

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Section: Discussionmentioning

confidence: 61%

Multiple forms of mRNA encoding human pregnancy-associated endometrial alpha 2-globulin, a beta-lactoglobulin homologue.

Garde

Bell

Eperon

1991

Proc. Natl. Acad. Sci. U.S.A.

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“…The nucleotide and inferred amino acid sequences of sheep (Gaye, Hue-Delahaie, Mercier et al 1986) and cow (Jamieson, Vandeyar, Kang et al 1987) Tissue culture conditions…”

Section: Dna Sequencing and Sequence Analysismentioning

confidence: 99%

A marsupial β-lactoglobulin gene: characterization and prolactin-dependent expression

Collet¹,

Joseph²,

Nicholas³

1991

Journal of Molecular Endocrinology

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Analysis of the tammar wallaby beta-lactoglobulin cDNA and inferred amino acid sequences reveal extensive sequence divergence from the eutherian beta-lactoglobulins. Conserved residues include the cysteines and a number of individual amino acids involved in structure and ligand-binding. The only region of extended similarity is a heptapeptide sequence which may impart specificity to its interaction with a receptor protein. Northern analysis of total mammary RNA revealed two transcripts which result from differential utilization of polyadenylation signals. The concentration of beta-lactoglobulin mRNA increased in late lactation and correlates with increases in milk production and levels of milk fat. Quantification of beta-lactoglobulin mRNA levels in hormone-stimulated mammary gland explants from tammars in late pregnancy suggests that maximal induction of the gene is dependent on prolactin alone and that expression is not modulated by other hormones known to play a role in the initiation of lactation in eutherians.

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“…These requisite components are now available in the form of a 2.7-A-resolution structure which has been determined by X-ray analysis of the orthorhombic crystal form of BLGA (Papiz et al, 1986) in addition to an efficient method for producing modified forms of the protein (Jamieson et al, 1987;Batt et al, 1990). We describe improvements made to BLG which enhance its gelation properties and increase its sensitivity to chymosin and acid.…”

Section: Introductionmentioning

confidence: 97%