ArticleThe Biochemical journal1995
Long-range conformational effects of proteolytic removal of the last three residues of actin.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Actin's functional "switch": Constraining C-terminal conformational flexibility disrupts functionally important communication networks.The Journal of biological chemistry · 2026Article
- Acetylation of fission yeast tropomyosin does not promote differential association with cognate formins.Cytoskeleton (Hoboken, N.J.) · 2023Article
- Myopathy-Sensitive G-Actin Segment 227-235 Is Involved in Salt-Induced Stabilization of Contacts within the Actin Filament.International journal of molecular sciences · 2021Article
- Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and fragmentation.PLoS biology · 2019Article
- Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.Nature structural & molecular biology · 2018Article
- Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- Structure of the F-actin-tropomyosin complex.Nature · 2015Article
- Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments.Nature structural & molecular biology · 2014Article
- Structural differences explain diverse functions of Plasmodium actins.PLoS pathogens · 2014Article
- ATP and ADP actin states.Biopolymers · 2013Article
- Structural states and dynamics of the D-loop in actin.Biophysical journal · 2012Article
- Subdomain location of mutations in cardiac actin correlate with type of functional change.PloS one · 2012Article
- Structural polymorphism in F-actin.Nature structural & molecular biology · 2010Article
- Allele-specific effects of human deafness gamma-actin mutations (DFNA20/26) on the actin/cofilin interaction.The Journal of biological chemistry · 2009Article
- Functional effects of nemaline myopathy mutations on human skeletal alpha-actin.The Journal of biological chemistry · 2008Article
- Role of actin C-terminus in regulation of striated muscle thin filament.Biophysical journal · 2008Article
- Solution properties of tetramethylrhodamine-modified G-actin.Biophysical journal · 2003Article
- Cofilin and DNase I affect the conformation of the small domain of actin.Biophysical journal · 2002Article
- Distinct structural changes detected by X-ray fiber diffraction in stabilization of F-actin by lowering pH and increasing ionic strength.Biophysical journal · 2001Article
- Divalent cation-, nucleotide-, and polymerization-dependent changes in the conformation of subdomain 2 of actin.Biophysical journal · 1999Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Truncated derivatives of actin devoid of either the last two (actin-2C) or three residues (actin-3C) were used to study the role of the C-terminal segment in the polymerization of actin. The monomer critical concentration and polymerization rate increased in the order: intact actin < actin-2C < actin-3C. Conversely, the rate of hydrolysis of actin-bound ATP during spontaneous polymerization of Mg-actin decreased in the same order, so that, for actin-3C, the ATP hydrolysis significantly lagged behind the polymer growth. Probing the conformation of the nucleotide site in the monomer form by measuring the rates of the bound nucleotide exchange revealed a similar change upon removal of either the two or three residues from the C-terminus. The C-terminal truncation also resulted in a slight decrease in the rate of subtilisin cleavage of monomeric actin within the DNAse-I binding loop, whereas in F-actin subunits the susceptibility of this and of another site within this loop, specifically cleaved by a proteinase from Escherichia coli A2 strain, gradually increased upon sequential removal of the two and of the third residue from the C-terminus. From these and other observations made in this work it has been concluded that perturbation of the C-terminal structure in monomeric actin is transmitted to the cleft, where nucleotide and bivalent cation are bound, and to the DNAse-I binding loop on the top of subdomain 2. Further changes at these sites, observed on the polymer level, seem to result from elimination of the intersubunit contact between the C-terminal residues and the DNAse-I binding loop. It is suggested that formation of this contact plays an essential role in regulating the hydrolysis of actin-bound ATP associated with the polymerization process.
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