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Tdd-3, a tRNA gene-associated poly(A) retrotransposon from Dictyostelium discoideum (1998)

Winckler, T. ; Tschepke, C. ; de Hostos, E. L. ; [et al.]

Springer

Molecular genetics and genomics 257 (1998), S. 655-661

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ISSN: 1617-4623

Keywords: Key wordsDictyostelium ; tRNA genes ; Reverse transcription ; Retrotransposon ; Repetitive DNA

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The full-length 5218-bp sequence of the mobile genetic element Tdd-3 from Dictyostelium discoideum is described. Tdd-3 encodes two overlapping open reading frames (ORFs) flanked by non-redundant, untranslated regions. The deduced amino acid sequence of ORF2 is homologous to reverse transcriptases (RTs) encoded by the class of poly(A) retrotransposons. ORF2 also encodes a putative protein domain related to the family of apurinic/apyrimidinic (AP) endonucleases, whose retroelement-encoded homologs have recently been proposed to represent the integrase function of poly(A) retrotransposons. Comparison of several genomic Tdd-3 copies revealed that element insertion is orientation specific and occurs about 100 bp downstream of tRNA genes in the D. discoideum genome. These properties of Tdd-3 suggest that the element is a tRNA gene-associated poly(A) retroelement present in the D. discoideum genome. Analysis of several cloned cDNAs derived from Tdd-3-specific plus strand RNAs indicate that the element is transcribed and polyadenylated during the growth of D. discoideum cells.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s004380050694

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Coactosin, a 17 kDA F-actin binding protein from Dictyostelium discoideum (1993)

de Hostos, E. L. ; Bradtke, B. ; Lottspeich, F. ; [et al.]

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 26 (1993), S. 181-191

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ISSN: 0886-1544

Keywords: cytoskeleton ; actin-binding protein ; cofilin ; drebrin ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: A 17 kDa protein, designated as coactosin, has been purified from an actinmyosin complex reconstituted in vitro from a soluble fraction of Dictyostelium discoideum cells. The protein binds to F-actin in vitro without significantly altering its viscosity. Immunoblots labeled with monoclonal antibodies indicate that part of the protein is associated with the detergent-insoluble cytoskeleton. cDNA clones comprising the entire coding region of coactosin have been isolated from an expression library. The cDNA-derived amino-acid sequence reveals similarities of coactosin to the drebrins identified in neurons and to actin-binding proteins from other organisms, including yeast ABP1p, and yeast and vertebrate cofilins. © 1993 Wiley-Liss, Inc.

Additional Material: 6 Ill.