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C Jacq

Publications and source records attributed to C Jacq.

At least 55 records · Page 3Linked to original sources
PubMed1989

The bI4 RNA mitochondrial maturase of Saccharomyces cerevisiae can stimulate intra-chromosomal recombination in Escherichia coli.

When the bI4 RNA maturase, encoded by the fourth intron of the mitochondrial cytochrome b gene of Saccharomyces cerevisiae, was expressed in Escherichia coli, formation of intra-chromosomal Lac+ recombinants was stimulated threefold. This "hyper-rec" phenotype was recA as well as recBCD dependent. The most active form of the bI4 maturase stimulated homologous recombination whereas splicing deficient mutants of bI4 maturase were either deficient in or unable to stimulate homologous recombination.

DNA Nucleotidyltransferases↗
PubMed1989

Synthesis and function of the mitochondrial intron--encoded bI4 RNA maturase from Saccharomyces cerevisiae. Effects of upstream frame-shift mutations.

We have analyzed the expression and function of the intron-encoded bI4 maturase when frame-shift mutations in the upstream exon alter the translational process. By constructing secondary cis-acting mutations within the bI4 intron, we observed (1) that the bI4 maturase is still translated in the presence of the upstream mutation, albeit in very low amounts, and (2) that the limited amounts of bI4 maturase made under these conditions is no longer able to promote the splicing process of the aI4 intron. These observations, which further strengthen the maturase model, strongly suggest that bI4 maturase acts sequentially on the bI4 intron and then on the aI4 intron.

Base Sequence↗
PubMed1987

Efficient splicing of two yeast mitochondrial introns controlled by a nuclear-encoded maturase.

bI4 maturase encoded by the fourth intron of the yeast mitochondrial cytochrome b gene, controls the splicing of both the fourth intron of the cytochrome b gene and the fourth intron of the gene encoding subunit I of cytochrome oxidase. It has been shown previously that a cytoplasmically translated hybrid protein composed of the pre-sequence of subunit 9 of Neurospora ATPase fused to a part of the bI4 maturase can be guided to mitochondria where it could compensate maturase deficiencies. This in vivo complementation of maturase mutants can be easily estimated by restoration of respiration. This work examines the efficiency of different bI4 maturase constructions to restore respiration in different yeast maturase-deficient strains. It is shown that the N-terminal end of the bI4 maturase plays a crucial role in the maturase activity. Moreover, the 12 N-terminal amino acids of the mitochondrial outer membrane protein constitute the most efficient mitochondrial targeting sequence in this system. Surprisingly enough, it was found that the cytoplasmically translated bI4 maturase containing the 254 C-terminal amino acid coded by the intron open reading frame can complement maturase mutations without any added mitochondrial-targeting sequence.

Base Sequence↗
PubMed1986

A mitochondrial RNA maturase gene transferred to the yeast nucleus can control mitochondrial mRNA splicing.

bI4 maturase, encoded by the fourth intron of the yeast mitochondrial cytochrome b gene, controls the splicing of both the fourth intron of the cytochrome b gene and the fourth intron of the gene encoding subunit I of cytochrome oxidase. By fusing the encoding presequence of subunit 9 of the Neurospora ATPase to a restriction fragment containing the bI4 maturase coding sequence, we have constructed a hybrid gene that can be translated on yeast cytosolic ribosomes. The resulting protein is imported into mitochondria, which was revealed by its ability to restore to respiratory competence a yeast mutant defective in the bI4 maturase. Moreover, a protein reacting with antimaturase antibodies was detected in the mitochondria of the transformed cells; this imported maturase functioned similarly to the endogenous maturase.

Cell Compartmentation↗
PubMed1985

Role of the 5' hairpin structure in the splicing accuracy of the fourth intron of the yeast cob-box gene.

The splicing mechanism of the maturase-coding introns is poorly understood. We have systematically examined the phenotypes of a large number of revertants from the mitochondrial mutation G2457. This mutation results from a single base change near the 5' splicing site. We show here that this base change does not completely block the splicing of the intron but rather affects the specificity of the splicing process. We examine four classes of revertants which allow us to characterize the crucial role of a stem and loop structure in the accuracy of the intron excision process. An unexpected class of revertant suggests that other elements are involved in this mechanism. Reversion of G2457 can also occur via the excision in the mitochondrial genome of the intron coding sequence. These results are discussed in relation to the possible role fulfilled by the maturase in the control of intron splicing.

Animals↗
PubMed1984

Antibodies against a fused 'lacZ-yeast mitochondrial intron' gene product allow identification of the mRNA maturase encoded by the fourth intron of the yeast cob-box gene.

Several missense or nonsense mutations have been localized in the fourth intron open reading frame (ORF) of the yeast mitochondrial cytochrome b gene. These results and the phenotypes of mutants strongly suggested that a mRNA maturase, controlling the expression of both cytochrome b and cytochrome oxidase subunit I (COXI) genes, is encoded in this ORF. To investigate more directly the biosynthesis of mRNA maturase we raised antibodies against a part of the putative ORF translation product. For that purpose we inserted a fragment of the ORF sequence, in phase, into the C-terminal EcoRI site of lacZ gene. The hybrid gene was then expressed in Escherichia coli under the control of either the wild-type lac promoter or the thermoregulated lambda system PR/cI857. The hybrid protein was partially purified and antibodies were raised against it. These antibodies recognized a mitochondrially coded protein, p27, in intron mutants, whereas no such protein was detected in the wild-type cell. These results demonstrate that the p27 protein, previously shown to be associated with the mRNA maturase activity, is actually translated from the intron ORF. The autoregulated mRNA maturase synthesis model is discussed in relation to these results.

Base Sequence↗
PubMed1982

Single base substitution in an intron of oxidase gene compensates splicing defects of the cytochrome b gene.

An extragenic suppressor mutation, mim2-1, which compensates yeast mitochondrial mutants deficient in splicing of the cytochrome b gene, has been mapped and sequenced. The mutation is due to a single G leads to A transition in the long open reading frame of the fourth intron of the oxidase subunit one gene. It causes the replacement of a glutamic codon by a lysine codon and the expression of a novel mRNA maturase active in splicing. Evolution and regulatory connections between homologous introns of nonhomologous genes are discussed.

Base Sequence↗
PubMed1982

The cytochrome oxidase subunit I split gene in Saccharomyces cerevisiae: genetic and physical studies of the mtDNA segment encompassing the 'cytochrome b-homologous' intron.

We have constructed a refined genetic and physical map of 38 oxi3 mutations. With the help of the rho- clones derived from 'short' and 'long' genes, pairwise crosses between mutants, estimations of their reversion frequencies and analyses of mitochondrially synthesized proteins, we have characterized and localized several mutants in the exon A4 and in the intron aI4. We present genetic and physical evidence that in the 'long' gene the exon A5 is split into at least three quite distinct exons, A5-1, A5-2 and A5-3 where numerous mutations are localized. We suggest that a novel 56 Kd polypeptide, which accumulates in some cis-dominant oxi3- mutants results from the translation of the upstream exons and the downstream aI4 intron.

Base Sequence↗
PubMed1982

Critical sequences within mitochondrial introns: pleiotropic mRNA maturase and cis-dominant signals of the box intron controlling reductase and oxidase.

We have established the DNA sequence of nine yeast mutants that prevent the expression either of the split cytochrome b gene alone (five mutants) or of two split genes, the cytochrome b gene and the cytochrome oxidase subunit I gene (four mutants). All the mutations analyzed are localized in intron 14 of the cob-box gene. We have extended the concept of the intron-encoded mRNA maturase, already described for intron 12, to the intron 14, and have adduced evidence that this box7 pleiotropic maturase is involved in the splicing of two distant gene transcripts. Such a process may constitute a regulatory mechanism that coordinates the expression of two structurally nonhomologous genes encoding two metabolically related enzymes. Analyses of cis-dominant mutations reveal the role of signal sequences in the recognition of the intron RNA sequences to be excised. These signal sequences are localized near the exon-intron boundaries (box1), or quite distant from the splicing sites, either in the blocked reading frame (box2) or in the open reading frame (box9) of the intron. We believe that for the last sequence, a ribosomal recognition of the box9 signal could be involved in a regulatory mechanism of the splicing of the pre-mRNA.

Base Sequence↗
PubMed1982

Critical sequences within mitochondrial introns: cis-dominant mutations of the "cytochrome-b-like" intron of the oxidase gene.

We have established the DNA sequence of two cis-dominant mutations located in the fourth intron, a14, of the yeast mitochondrial gene oxi3. These mutations prevent the synthesis of subunit I of cytochrome oxidase. Both mutations affect a very short DNA sequence located several hundred base pairs from the intron-exon junctions. An identical sequence is found in the cob-box gene; and this sequence is critical for the excision of the cytochrome b intron. Our interpretation is that this short sequence represents a common signal that must be recognized by the box7-encoded mRNA maturase, in conjunction with the mitochondrial ribosome, to splice out the introns in the two nonhomologous genes, cob-box and oxi3.

Base Sequence↗
PubMed1982

Lactic deshydrogenase isoenzymes in the ocular tissues and liquids.

Lactic deshydrogenase isoenzymes in different parts of the ocular tissues and humors were analyzed. An appreciation in crossing of the lactic deshydrogenase concentration was indicated. In the human eye, the largest quantities of lactic deshydrogenase were found in the cornea and in the vitreous and aqueous humors, where isoenzymes 3, 4, and 5 are the most numerous. Lactic deshydrogenase was found in small quantities only in the conjunctiva and in the lacrimal gland. In the bovine eye, the proportion of isoenzymes is different. The chemical constitution of human serum isoenzymes seems to differ from that of the tissues and liquids in the bovine eye (their mobility is different). Therefore, the results obtained with bovine eyes cannot be applied to human eyes. The largest quantity of lacrimal lactic deshydrogenase isoenzymes comes from the cornea, any recent corneal lesion causing an increase in isoenzyme 4.

Animals↗
PubMed1981

Splice points of the third intron in the yeast mitochondrial cytochrome b gene.

We report the nucleotide sequences at the splicing junctions of intron 13 of the cytochrome b (box) "long" gene of the mitochondrion of Saccharomyces cerevisiae and compare them with the homologous sequences in Aspergillus nidulans. The two introns occupy exactly the same position and display an open reading frame in phase with the preceding exon at the 5' end and a blocked region at the 3' end.

Base Sequence↗
PubMed1980

[New mechanism for regulation of genetic expression].

DNA sequence studies of mutated and wild type alleles of an intron in the mosaic mitochondrial gene for cytochrome b have revealed the possible existence of a protein coded in the intron and involved in RNA splicing. This protein would be endowed with properties of intrinsic autotomy of its own messenger RNA.

Amino Acid Sequence↗
PubMed1980

Sequence of introns and flanking exons in wild-type and box3 mutants of cytochrome b reveals an interlaced splicing protein coded by an intron.

We have determined the DNA sequence of the wild type and mutated introns as well as their flanking exons in the yeast mitochondrial gene specifying cytochrome b. The second intron (box3) encodes a trans-acting protein "mRNA maturase" responsible for splicing and maturation of cytochrome b mRNA. This protein is interlaced with cytochrome b exon sequences. Its biosynthesis is subject to a negative feedback which may constitute a regulatory mechanism for the expression of split genes.

Base Sequence↗
PubMed1980

[Conjunctival fungal flora of healthy people (author's transl)].

A study has been carried out on three groups of subjects. The first group, living in the surrounding of Paris, without inflammatory diseases and without local treatments, gives a contamination rate of 3,92%, which is well balanced with yeasts and fungoid growth myceliums. The principal isolated species were: Penicillium, Aspergillus, Candida, Rhodotorula. The second group with local treatment by mercurothiolate natrium was sterile. The third group, whose subjects had nearly a daily cultivation, allows to establish that: -- The conjunctival fungic flora is variable with time, and differ of a eye from the other for a given subject and its continuance is short; -- The subject contamination seems to be different according to the quality of the immune defenses, the less effective showing always yeasts and fungoid growth myceliums, the other ones slightly infected and only with fungoid growth myceliums; -- The contamination rate seems to be directly related to the intensity of the surrounding atmosphere agitation.

Aspergillus↗
PubMed1979

Inserted sequence in the mitochondrial 23S ribosomal RNA gene of the yeast Saccharomyces cerevisiae.

The sequence organization of the yeast mit-DNA region carrying the large ribosomal RNA gene and the polar locus omega was examined. Hybridization studies using rho- deletion mutants and electron microscopy of the heteroduplexes formed between 23S rRNA and the appropriate restriction fragments, lead to the conclusion that the 23S rRNA1 gene of the omega+ strains is split by an insertion sequence of 1,000-1,100 bp. In contrast, no detactable insertion was found in the 23S rRNA gene of the omega- strains. The size and the location of the insert found in the 23S rRNA gene of the omega+ strains appear to be identical to those of the sequence delta which had previously been found to characterize the difference (at the omega locus) between the mitDNA of the wild type strains carrying the omega+ or omega- alleles (Jacq et al., 1977).

Base Sequence↗
PubMed1979

Characterization of a histone-like protein extracted from yeast mitochondria.

Analysis of proteins isolated by affinity chromatography on DNA-cellulose from highly purified yeast mitochondria shows that these organelles do not contain histones but have in abundance a DNA-binding protein of 20,000 daltons. The purification yield of this protein, called HM, indicates that mitochondria have at least an equal mass of HM relative to DNA. The amino acid composition and its electrophoretic characterization reveal that HM, rich in lysine, is slightly basic and heat stable. HM appears to be coded by the yeast nucleus, as shown by its presence in several "petite" mutants. We have shown that HM, like histones or histone-like proteins, is able to introduce superhelical turns into circular relaxed DNA in the presence of a nicking-closing activity.

Amino Acids↗