Biomedical subjects

M A Marra

Publications and source records attributed to M A Marra.

23 records · Page 2Linked to original sources

PubMed1994

The Caenorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins.

Mutations in the unc-60 gene of the nematode Caenorhabditis elegans result in paralysis. The thin filaments of the muscle cells are severely disorganized and not bundled with myosin into functional contractile units. Here we report the cloning and sequence of unc-60. Two unc-60 transcripts, 1.3 and 0.7 kb in size, were detected. The transcripts share a single exon encoding only the initial methionine, yet encode proteins with homologous sequences. The predicted protein products are 165 and 152 amino acids in length and their sequences are 38% identical. Both proteins are homologous to a family of actin depolymerizing proteins identified in vertebrate, plant and protozoan systems. We propose that the unc-60 locus encodes proteins that depolymerize growing actin filaments in muscle cells, and that these proteins are required for the assembly of actin filaments into the contractile myofilament lattice of C. elegans muscle. unc-60 has an essential function in development, since one unc-60 allele, s1586, has a recessive lethal phenotype. Our characterization of s1586 has shown that it is a small deletion which disrupts both coding regions.

Amino Acid Sequence↗

PubMed1994

Recovery of duplications by drug resistance selection in Caenorhabditis elegans.

We have devised a scheme that facilitates rapid screening for duplications of essential loci. Our scheme takes advantage of the lev-1(x22) mutation, which confers resistance in a recessive fashion to the potent anthelmintic levamisole. We have tested our methodology by recovering two gamma ray induced duplications of let-56, the first essential gene to the left of unc-22. One of the duplications is attached to the fourth chromosome. The other duplication is attached to the X chromosome. This duplication contains a functional copy of the unc-22 gene, as well as functional copies of several essential loci adjacent to unc-22. Results we have obtained during analysis of this duplication are compatible with the notion that the copy of the unc-22 gene located on the duplication is subject to X chromosome dosage compensation.

Animals↗

PubMed1993

Molecular analysis of two genes between let-653 and let-56 in the unc-22(IV) region of Caenorhabditis elegans.

A previous study of genomic organization described the identification of nine potential coding regions in 150 kb of genomic DNA from the unc-22(IV) region of Caenorhabditis elegans. In this study, we focus on the genomic organization of a small interval of 0.1 map unit bordered on the right by unc-22 and on the left by the left-hand breakpoints of the deficiencies sDf9, sDf19 and sDf65. This small interval at present contains a single mutagenically defined locus, the essential gene let-56. The cosmid C11F2 has previously been used to rescue let-56. Therefore, at least some of C11F2 must reside in the interval. In this paper, we report the characterization of two coding elements that reside on C11F2. Analysis of nucleotide sequence data obtained from cDNAs and cosmid subclones revealed that one of the coding elements closely resembles aromatic amino acid decarboxylases from several species. The other of these coding elements was found to closely resemble a human growth factor activatable Na+/H+ antiporter. Paris of oligonucleotide primers, predicted from both coding elements, have been used in PCR experiments to position these coding elements between the left breakpoint of sDf19 and the left breakpoint of sDf65, between the essential genes let-653 and let-56.

Amino Acid Sequence↗

PubMed1993

The use of deficiencies to determine essential gene content in the let-56-unc-22 region of Caenorhabditis elegans.

We have investigated the possibility of using the polymerase chain reaction to detect deletions of coding elements in the unc-22-let-56 interval on chromosome IV in the nematode Caenorhabditis elegans. Our analysis of approximately 13 kb of genomic sequence immediately to the left of the unc-22 gene resulted in the identification of four possible genes. Partial cDNAs have been identified for three of them. To determine whether any of these coding elements are essential for development, we required a method for the induction and selection of mutations in these elements. Our approach was to identify a set of formaldehyde and gamma radiation induced unc-22 mutations that mapped to the unc-22-let-56 region, and then employ polymerase chain reaction methodology to identify deficiencies that affected one or more of the four identified coding elements. Two small deficiencies were identified in this manner. Characterization of these deficiencies shows that there are no coding elements between unc-22 and let-56 (the nearest mutationally identified gene to the left of unc-22), which are required in development under laboratory conditions. We conclude that the polymerase chain reaction is a practical tool for the detection of deletions of coding elements identified in this region, and that characterization of such deficiencies provides a method for assessing whether or not these elements are required for development.

Amino Acid Sequence↗

PubMedDate not supplied

Isolation of Leishmania sp. from aqueous humor of a patient with cutaneous disseminated leishmaniasis and bilateral iridocyclitis (preliminary report).

The authors report an uncommon case of leishmaniasis with disseminated cutaneous lesions, systemic manifestations and ocular involvement, the latter being characterized by bilateral nongranulomatous iridocyclitis. The severity of the ophthalmologic lesions and its unresponsiveness to therapy (in spite of satisfactory regression of both systemic and cutaneous manifestations) lead to a needle aspiration of the anterior eye chamber content. From this material Leishmania sp was isolated. To our knowledge this is the first time that Leishmania has been shown into the ocular globe.

Amphotericin B↗