Isolation and characterization of a cDNA that encodes mouse fibroblast tropomyosin isoform 2

1988 ◽  
Vol 8 (12) ◽  
pp. 5561-5565
Author(s):  
K Takenaga ◽  
Y Nakamura ◽  
K Tokunaga ◽  
H Kageyama ◽  
S Sakiyama

We isolated and characterized a cDNA clone encoding tropomyosin isoform 2 (TM2) from a mouse fibroblast cDNA library. TM2 was found to contain 284 amino acids and was closely related to the rat smooth and skeletal muscle alpha-TMs and the human fibroblast TM3. The amino acid sequence of TM2 showed a nearly complete match with that of human fibroblast TM3 except for the region from amino acids 189 to 213, the sequence of which was identical to those of rat smooth and skeletal muscle alpha-TMs. These results suggest that TM2 is expressed from the same gene that encodes the smooth muscle alpha-TM, the skeletal muscle alpha-TM, and TM3 via an alternative RNA-splicing mechanism. Comparison of the expression of TM2 mRNA in low-metastatic Lewis lung carcinoma P29 cells and high-metastatic D6 cells revealed that it was significantly less in D6 cells than in P29 cells, supporting our previous observations (K. Takenaga, Y. Nakamura, and S. Sakiyama, Mol. Cell. Biol. 8:3934-3937, 1988) at the protein level.

1988 ◽  
Vol 8 (12) ◽  
pp. 5561-5565 ◽  
Author(s):  
K Takenaga ◽  
Y Nakamura ◽  
K Tokunaga ◽  
H Kageyama ◽  
S Sakiyama

We isolated and characterized a cDNA clone encoding tropomyosin isoform 2 (TM2) from a mouse fibroblast cDNA library. TM2 was found to contain 284 amino acids and was closely related to the rat smooth and skeletal muscle alpha-TMs and the human fibroblast TM3. The amino acid sequence of TM2 showed a nearly complete match with that of human fibroblast TM3 except for the region from amino acids 189 to 213, the sequence of which was identical to those of rat smooth and skeletal muscle alpha-TMs. These results suggest that TM2 is expressed from the same gene that encodes the smooth muscle alpha-TM, the skeletal muscle alpha-TM, and TM3 via an alternative RNA-splicing mechanism. Comparison of the expression of TM2 mRNA in low-metastatic Lewis lung carcinoma P29 cells and high-metastatic D6 cells revealed that it was significantly less in D6 cells than in P29 cells, supporting our previous observations (K. Takenaga, Y. Nakamura, and S. Sakiyama, Mol. Cell. Biol. 8:3934-3937, 1988) at the protein level.


1990 ◽  
Vol 2 (4) ◽  
pp. 151-158 ◽  
Author(s):  
Nicholas A. Bruno ◽  
Lea Ann Carver ◽  
Doris L. Slate

1981 ◽  
Vol 3 (6) ◽  
pp. 1186-1195 ◽  
Author(s):  
R. Derynck ◽  
R. Devos ◽  
E. Remaut ◽  
E. Saman ◽  
P. Stanssens ◽  
...  

1999 ◽  
Vol 181 (14) ◽  
pp. 4397-4403 ◽  
Author(s):  
Casper Jørgensen ◽  
Gert Dandanell

ABSTRACT In this work, the LysR-type protein XapR has been subjected to a mutational analysis. XapR regulates the expression of xanthosine phosphorylase (XapA), a purine nucleoside phosphorylase inEscherichia coli. In the wild type, full expression of XapA requires both a functional XapR protein and the inducer xanthosine. Here we show that deoxyinosine can also function as an inducer in the wild type, although not to the same extent as xanthosine. We have isolated and characterized in detail the mutants that can be induced by other nucleosides as well as xanthosine. Sequencing of the mutants has revealed that two regions in XapR are important for correct interactions between the inducer and XapR. One region is defined by amino acids 104 and 132, and the other region, containing most of the isolated mutations, is found between amino acids 203 and 210. These regions, when modelled into the three-dimensional structure of CysB from Klebsiella aerogenes, are placed close together and are most probably directly involved in binding the inducer xanthosine.


1962 ◽  
Vol 40 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Anima Devi

RNA from rat ocular lens has been isolated by a method based on Kirby's original procedure (7), but greatly modified so as to avoid any degradation of RNA by RNase during the process of its extraction from lenses. The absorption at 260 mμ of a 1.0% solution of this purified material in a 1-cm cell is 1.95. Its N/P ratio is 1.58. It has 20 to 25% activity of that of yeast-soluble RNA in accepting activated amino acids. When this RNA (like all other RNA's) is heated and cooled the polynucleotide chain can again form loops, thus suggesting a randomly coiled structure for this RNA. On the other hand, DNA preparations from calf thymus, rat liver, and E. coli showed irreversible changes when heated and cooled.


Author(s):  
Diantha van de Vlekkert ◽  
Xiaohui Qiu ◽  
Ida Annunziata ◽  
Alessandra d'Azzo

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