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Study · In vitro (cell-free) · 1996

4 results

Identification of contact sites in the actin-thymosin beta 4 complex by distance-dependent thiol cross-linking.

Reichert A, Heintz D, Echner H, Voelter W, Faulstich H

The Journal of biological chemistry1 Jan 1996Cited by 16 (Europe PMC)

PMID8576116 (opens in a new tab)DOI10.1074/jbc.271.3.1301 (opens in a new tab)PepBankPUB-08576116
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Summary

Binding sites of actin and thymosin beta 4 were investigated using a set of bifunctional thiol-specific reagents, which allowed the insertion of cross-linkers of defined lengths between cysteine residues of the complexed proteins. After the cross-linkers were attached to actin specifically at either Cys10, Cys374, or the sulfur atom of the ATP analog adenosine 5'-O-(thiotriphosphate) (ATP gamma S), the actin derivatives were reacted with synthetic thymosin beta 4 analogs containing a cysteine at one of the positions 6, 17, 28, 34, and 40. Immediate cross-linking as followed by UV spectroscopy was found for Cys374 of actin and Cys6 of thymosin beta 4, indicating that the N terminus of thymosin beta 4 is in close proximity (< or = 9.2 A) to the C terminus of actin. In contrast, only insignificant reactivity was measured for all thymosin beta 4 analogs when the cross-linkers were anchored at Cys10 of actin. A second contact site was identified by cross-linking of Cys17 and Cys28 in thymosin beta 4 with the ATP gamma S derivative bound to actin, indicating that the hexamotif of thymosin beta 4 (positions 17-22) is in close proximity (< or = 9.2 A) to the nucleotide. The importance of the amino acids 17 and 28 in thymosin beta 4 for the interaction with actin was emphasized by the finding that thymosin analogs containing cysteine in these positions exhibited strongly reduced abilities to inhibit actin polymerization.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study4

4 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Activity measurement

    Immediate cross-linking was found between Cys374 of actin and Cys6 of thymosin beta‑4, which puts the N terminus of thymosin beta‑4 close to the C terminus of actin.

    In plain wordsIn lab tests, the start of thymosin beta‑4 sat very close to the end of actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableCross-linking of thymosin beta 4 Cys6 to actin Cys374
    Study

    n: not reported in source

    purified proteins and synthetic peptides
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Immediate cross-linking as followed by UV spectroscopy was found for Cys374 of actin and Cys6 of thymosin beta 4, indicating that the N terminus of thymosin beta 4 is in close proximity (< or = 9.2 A) to the C terminus of actin.
    2 context sentences
    Summary · context
    Binding sites of actin and thymosin beta 4 were investigated using a set of bifunctional thiol-specific reagents, which allowed the insertion of cross-linkers of defined lengths between cysteine residues of the complexed proteins.
    Summary · context
    After the cross-linkers were attached to actin specifically at either Cys10, Cys374, or the sulfur atom of the ATP analog adenosine 5'-O-(thiotriphosphate) (ATP gamma S), the actin derivatives were reacted with synthetic thymosin beta 4 analogs containing a cysteine at one of the positions 6, 17, 28, 34, and 40.
  2. 02LabIn vitro (cell-free)Activity measurement

    Only insignificant reactivity was measured for all thymosin beta‑4 analogs when the cross-linkers were anchored at Cys10 of actin.

    In plain wordsIn lab tests, the thymosin beta‑4 analogs reacted very little with one actin site (Cys10).

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changeCross-linking of thymosin beta 4 analogs to actin Cys10
    Study

    n: not reported in source

    purified proteins and synthetic peptides
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In contrast, only insignificant reactivity was measured for all thymosin beta 4 analogs when the cross-linkers were anchored at Cys10 of actin.
    2 context sentences
    Summary · context
    Binding sites of actin and thymosin beta 4 were investigated using a set of bifunctional thiol-specific reagents, which allowed the insertion of cross-linkers of defined lengths between cysteine residues of the complexed proteins.
    Summary · context
    After the cross-linkers were attached to actin specifically at either Cys10, Cys374, or the sulfur atom of the ATP analog adenosine 5'-O-(thiotriphosphate) (ATP gamma S), the actin derivatives were reacted with synthetic thymosin beta 4 analogs containing a cysteine at one of the positions 6, 17, 28, 34, and 40.
  3. 03LabIn vitro (cell-free)Activity measurement

    Cross-linking of Cys17 and Cys28 in thymosin beta‑4 with the ATP gamma S derivative bound to actin shows that the hexamotif of thymosin beta‑4 is close to the nucleotide.

    In plain wordsIn lab tests, a middle part of thymosin beta‑4 sat close to the nucleotide bound to actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableContact between thymosin beta 4 hexamotif and actin-bound nucleotide
    Study

    n: not reported in source

    purified proteins and synthetic peptides
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    A second contact site was identified by cross-linking of Cys17 and Cys28 in thymosin beta 4 with the ATP gamma S derivative bound to actin, indicating that the hexamotif of thymosin beta 4 (positions 17-22) is in close proximity (< or = 9.2 A) to the nucleotide.
    2 context sentences
    Summary · context
    Binding sites of actin and thymosin beta 4 were investigated using a set of bifunctional thiol-specific reagents, which allowed the insertion of cross-linkers of defined lengths between cysteine residues of the complexed proteins.
    Summary · context
    After the cross-linkers were attached to actin specifically at either Cys10, Cys374, or the sulfur atom of the ATP analog adenosine 5'-O-(thiotriphosphate) (ATP gamma S), the actin derivatives were reacted with synthetic thymosin beta 4 analogs containing a cysteine at one of the positions 6, 17, 28, 34, and 40.
  4. 04LabIn vitro (cell-free)Activity measurement

    Thymosin analogs with cysteine at positions 17 and 28 had strongly reduced ability to inhibit actin polymerization.

    In plain wordsIn lab tests, thymosin analogs changed at two key positions were much weaker at blocking actin polymerization.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    DecreaseInhibition of actin polymerization by thymosin analogs with Cys at positions 17 and 28
    Study

    n: not reported in source

    purified proteins and synthetic peptides
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The importance of the amino acids 17 and 28 in thymosin beta 4 for the interaction with actin was emphasized by the finding that thymosin analogs containing cysteine in these positions exhibited strongly reduced abilities to inhibit actin polymerization.
    2 context sentences
    Summary · context
    Binding sites of actin and thymosin beta 4 were investigated using a set of bifunctional thiol-specific reagents, which allowed the insertion of cross-linkers of defined lengths between cysteine residues of the complexed proteins.
    Summary · context
    After the cross-linkers were attached to actin specifically at either Cys10, Cys374, or the sulfur atom of the ATP analog adenosine 5'-O-(thiotriphosphate) (ATP gamma S), the actin derivatives were reacted with synthetic thymosin beta 4 analogs containing a cysteine at one of the positions 6, 17, 28, 34, and 40.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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