3‘-5‘ Exonuclease of Klenow Fragment:  Role of Amino Acid Residues within the Single-Stranded DNA Binding Region in Exonucleolysis and Duplex DNA Melting†

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pp. 3943-3951 ◽  
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Elizabeth H. Z. Thompson ◽  
Olga Potapova ◽  
Xiaojun Chen Sun ◽  
Catherine M. Joyce ◽  
...  
2002 ◽  
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pp. 50643-50653 ◽  
Author(s):  
Lisa F. Rezende ◽  
Thomas Hollis ◽  
Tom Ellenberger ◽  
Charles C. Richardson

Biochemistry ◽  
1997 ◽  
Vol 36 (14) ◽  
pp. 4080-4088 ◽  
Author(s):  
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M. L. Dodson ◽  
R. Stephen Lloyd

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Artemiy S. Bakman ◽  
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Olga S. Fedorova ◽  
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Claire Martin ◽  
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Esmeralda Parić ◽  
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...  

Tropomyosins (Tpms) have been described as master regulators of actin, with Tpm3 products shown to be involved in early developmental processes, and the Tpm3 isoform Tpm3.1 controlling changes in the size of neuronal growth cones and neurite growth. Here, we used primary mouse hippocampal neurons of C57/Bl6 wild type and Bl6Tpm3flox transgenic mice to carry out morphometric analyses in response to the absence of Tpm3 products, as well as to investigate the effect of C-terminal truncation on the ability of Tpm3.1 to modulate neuronal morphogenesis. We found that the knock-out of Tpm3 leads to decreased neurite length and complexity, and that the deletion of two amino acid residues at the C-terminus of Tpm3.1 leads to more detrimental changes in neurite morphology than the deletion of six amino acid residues. We also found that Tpm3.1 that lacks the 6 C-terminal amino acid residues does not associate with stress fibres, does not segregate to the tips of neurites, and does not impact the amount of the filamentous actin pool at the axonal growth cones, as opposed to Tpm3.1, which lacks the two C-terminal amino acid residues. Our study provides further insight into the role of both Tpm3 products and the C-terminus of Tpm3.1, and it forms the basis for future studies that aim to identify the molecular mechanisms underlying Tpm3.1 targeting to different subcellular compartments.


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