A single locus in the mouse encodes both myosin light chains 1 and 3, a second locus corresponds to a related pseudogene

Robert, Benoît; Daubas, Philippe; Akimenko, Marie‐Andrée; Cohen, Arlette; Garner, Ian; Guénet, Jean-Louis; Buckingham, Margaret

doi:10.1016/0092-8674(84)90198-3

Cited by 246 publications

(121 citation statements)

References 64 publications

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“…Whatever the mechanism, these data suggest that such effects may regulate gene expression in eucaryotic cells. A number of loci have been described that can be transcribed from two proxi-mal promoters including a muscle myosin light chain gene (see Robert et al, 1984 (Schwartz et al, 1986). This situation differs from that which we observe in that the level of a-cardiac actin mRNA in these hypertrophic hearts remains high.…”

Section: Discussioncontrasting

confidence: 54%

A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

Garner¹,

Minty²,

Alonso³

et al. 1986

The EMBO Journal

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We describe the structure and transcriptional activity of the 5′ portion of the alpha‐cardiac actin gene of BALB/c mice. Southern blotting and DNA sequencing reveal that the promoter and first three exons of the gene are present as perfect repeats in a direct duplication of 9.5 kbp situated immediately upstream of the gene. Both promoters are active in adult cardiac tissue. Transcripts from the partial gene duplication give rise to novel RNAs that are spliced correctly in the actin region and polyadenylated. The level of mature alpha‐cardiac actin mRNA is only 16.5% that found in mice that do not possess the duplication. This is due, at least in part, to interference at the transcriptional level. Transcripts from the alpha‐skeletal actin gene accumulate to abnormally high levels in the hearts of such mutant mice. This result suggests tight regulatory coupling for this actin gene pair.

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Section: Discussioncontrasting

confidence: 54%

A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

Garner¹,

Minty²,

Alonso³

et al. 1986

The EMBO Journal

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“…5' UTR of mouse MLClF mRNA (Robert et al, 1984), probe length 60 bases. This sequence is available from EMBLIGenBanWDDJB under accession number K02237.…”

Section: Probe Preparationmentioning

confidence: 99%

Modulation of contractile protein gene expression in fetal murine crural muscles: Emergence of muscle diversity

Ontell

Sopper

Lyons

et al. 1993

Developmental Dynamics

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The modulation of contractile protein gene expression in mouse crural muscles (i.e., muscles located in the region between the knee and ankle) during the fetal period (defined as 15 days gestation to birth), resulting in diversity among and within these muscles, has been evaluated with in situ hybridization and correlated with morphogenetic events in the extensor digitorum longus and soleus muscles. During the fetal period extensive secondary myotube formation occurs in the crural muscles, and the myotubes become innervated (Ontell and Kozeka [1984a,bl Am.

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“…Further analysis of the genomic sequences will solve this problem. The selective use of exons has been described for the generation of muscular protein isoforms with distinct NH2-terminal peptides [24] but we present the first sequence data documenting such a mechanism in the generation of tissue-specific isoenzymes. The case of porphobilinogen deaminase is probably not unique since previous studies have demonstrated that liver L and red cells L' isoforms of pyruvate kinase are also encoded by two mRNAs from a single gene [25].…”

Section: Lys-asp-gly-gln-leu-tyr-leu-thr-gly-gly-val-trp-ser-leu-asp-mentioning

confidence: 99%

Tissue‐specific expression of porphobilinogen deaminase

Grandchamp

Verneuil

Beaumont

et al. 1987

European Journal of Biochemistry

198

109

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Porphobilinogen deaminase (hydroxymethylbilane synthase; EC 4.3.1.8), the third enzyme of the heme biosynthetic pathway, catalyzes the stepwise condensation of four porphobilinogen units to yield hydroxymethylbilan, which is in turn converted to uroporphyrinogen III by cosynthetase. We compared the apparent molecular mass of porphobilinogen deaminase from erythropoietic and from non‐erythropoietic cells by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and immune‐blotting. The results indicate that two isoforms of porphobilinogen deaminase can be distinguished and differ by 2000 Da. Analysis of cell‐free translation products directed by mRNAs from human erythropoietic spleen and from human liver demonstrates that the two isoforms of porphobilinogen deaminase are encoded by distinct messenger RNAs. We cloned and sequenced cDNAs complementary to the non‐erythropoietic form of porphobilinogen deaminase encoding RNA. Comparison of these sequences to that of human erythropoietic mRNA [Raich et al. (1986) Nucleic Acids Res. 14, 5955–5968] revealed that the two mRNA species differ by their 5′ extremity. From the mRNA sequences we could deduce that an additional peptide of 17 amino acid residues at the NH2 terminus of the non‐erythropoietic isoform of porphobilinogen deaminase accounts for its higher molecular mass. RNase mapping experiments demonstrate that the two porphobilinogen deaminase mRNAs are distributed according to a strict tissue‐specificity, the erythropoietic form being restricted to erythropoietic cells. We propose that a single porphobilinogen deaminase gene is transcribed from two different promoters, yielding the two forms of porphobilinogendeaminase mRNAs. Our present finding may have some relevance for further understanding the porphobilinogen deaminase deficiency in certain cases of acute intermittent porphyria with an enzymatic defect restricted in non‐erythropoietic cells.

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A single locus in the mouse encodes both myosin light chains 1 and 3, a second locus corresponds to a related pseudogene

Cited by 246 publications

References 64 publications

A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

Modulation of contractile protein gene expression in fetal murine crural muscles: Emergence of muscle diversity

Tissue‐specific expression of porphobilinogen deaminase

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