scholarly journals The Role of the Carboxyl-terminal Amino Acid Residues inEscherichia coliDNA Topoisomerase III-mediated Catalysis

1996 ◽  
Vol 271 (15) ◽  
pp. 9039-9045 ◽  
Author(s):  
Hong Liang Zhang ◽  
Swati Malpure ◽  
Zhiyu Li ◽  
Hiroshi Hiasa ◽  
Russell J. DiGate
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Topoisomerase Iii ◽  
Terminal Amino ◽  
Carboxyl Terminal ◽  
Mediated Catalysis

scholarly journals Deletion of the Actin-Associated Tropomyosin Tpm3 Leads to Reduced Cell Complexity in Cultured Hippocampal Neurons—New Insights into the Role of the C-Terminal Region of Tpm3.1

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 715
Author(s):  
Tamara Tomanić ◽  
Claire Martin ◽  
Holly Stefen ◽  
Esmeralda Parić ◽  
Peter Gunning ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hippocampal Neurons ◽  
Molecular Mechanisms ◽  
Growth Cones ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
C Terminus ◽  
Primary Mouse ◽  
Terminal Amino

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.

The role of C-terminal amino acid residues of a Δ6-fatty acid desaturase from blackcurrant

2013 ◽  
Vol 431 (4) ◽  
pp. 675-679 ◽  
Author(s):  
Li-Ying Song ◽  
Wan-Xiang Lu ◽  
Jun Hu ◽  
Wei-Bo Yin ◽  
Yu-Hong Chen ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Fatty Acid Desaturase ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Terminal Amino

The Carboxyl-Terminal Amino Acid Sequence of Streptomyces griseus Protease A

1972 ◽  
Vol 50 (6) ◽  
pp. 589-599 ◽  
Author(s):  
Peter Johnson ◽  
Lawrence B. Smillie
Keyword(s):  
Amino Acid ◽  
Cyanogen Bromide ◽  
Streptomyces Griseus ◽  
Amino Acid Residues ◽  
Disulfide Bridges ◽  
Terminal Amino Acid ◽  
Hydrophobic Residues ◽  
Terminal Amino ◽  
Carboxyl Terminal ◽  
Terminal Amino Acid Sequence

The sequence of 62 amino acid residues from the COOH-terminus of Streptomyces griseus Protease A has been established from peptic peptides previously described and from α-lytic protease and tryptic digests of the aminoethylated cyanogen bromide COOH-terminal fragment of the protein. This sequence includes one of the two disulfide bridges of the protein and the characteristic Asp–Ser–Gly sequence of this class of protease. When comparisons of residue similarity are made, the Streptomyces griseus Protease A sequence appears to be more similar (53% extent of similarity) to that of Myxobacter α-lytic protease than to any other protease. Both proteins appear to have common insertions at residue positions 189 and 192, and have characteristic clusters of hydrophobic residues near the COOH-terminus which are also present in other Asp–Ser–Gly proteases.

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