Identification of a short sequence essential for actin binding by Dictyostelium ABP-120

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Abstract

Tryptic digestion of ABP-120, an actin cross-linking protein from Dictyostelium discoideum, generates a ladder of peptides differing in molecular mass by 13,000 daltons, indicating a structural repeat within the molecule. A number of peptides bind actin with the smallest having a molecular mass of 17,000 daltons (T17). Our sedimentation assays also show that a peptide of 14,000 daltons does not bind actin. Using the full-length cDNA sequence (Noegel, A., Rapp, S., Lottspeich, F., Schleicher, M., and Stewart, M. (1989) J. Cell Biol. 109, 607-618) and protein sequencing techniques, we have determined that T17 begins at residue 89 while T14 begins at residue 116. Therefore we have localized 27 amino acids which are essential for actin binding activity. This region is at the end of the molecule, distal from the repetitive β-sheet region predicted from the cDNA sequence, and displays high sequence identity with regions in the N termini of ABP/ filamin, dystrophin, β-spectrin, and α-actinin.

Original languageEnglish (US)
Pages (from-to)9236-9240
Number of pages5
JournalJournal of Biological Chemistry
Volume265
Issue number16
StatePublished - Jun 5 1990

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Dictyostelium
Actins
Molecular mass
Peptides
Complementary DNA
Filamins
Actinin
Spectrin
Dystrophin
Molecules
Essential Amino Acids
Nucleic Acid Repetitive Sequences
Protein Sequence Analysis
Ladders
Sedimentation
Digestion
Assays
Proteins
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of a short sequence essential for actin binding by Dictyostelium ABP-120. / Bresnick, Anne R.; Warren, Vivien; Condeelis, John S.

In: Journal of Biological Chemistry, Vol. 265, No. 16, 05.06.1990, p. 9236-9240.

Research output: Contribution to journalArticle

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N2 - Tryptic digestion of ABP-120, an actin cross-linking protein from Dictyostelium discoideum, generates a ladder of peptides differing in molecular mass by 13,000 daltons, indicating a structural repeat within the molecule. A number of peptides bind actin with the smallest having a molecular mass of 17,000 daltons (T17). Our sedimentation assays also show that a peptide of 14,000 daltons does not bind actin. Using the full-length cDNA sequence (Noegel, A., Rapp, S., Lottspeich, F., Schleicher, M., and Stewart, M. (1989) J. Cell Biol. 109, 607-618) and protein sequencing techniques, we have determined that T17 begins at residue 89 while T14 begins at residue 116. Therefore we have localized 27 amino acids which are essential for actin binding activity. This region is at the end of the molecule, distal from the repetitive β-sheet region predicted from the cDNA sequence, and displays high sequence identity with regions in the N termini of ABP/ filamin, dystrophin, β-spectrin, and α-actinin.

AB - Tryptic digestion of ABP-120, an actin cross-linking protein from Dictyostelium discoideum, generates a ladder of peptides differing in molecular mass by 13,000 daltons, indicating a structural repeat within the molecule. A number of peptides bind actin with the smallest having a molecular mass of 17,000 daltons (T17). Our sedimentation assays also show that a peptide of 14,000 daltons does not bind actin. Using the full-length cDNA sequence (Noegel, A., Rapp, S., Lottspeich, F., Schleicher, M., and Stewart, M. (1989) J. Cell Biol. 109, 607-618) and protein sequencing techniques, we have determined that T17 begins at residue 89 while T14 begins at residue 116. Therefore we have localized 27 amino acids which are essential for actin binding activity. This region is at the end of the molecule, distal from the repetitive β-sheet region predicted from the cDNA sequence, and displays high sequence identity with regions in the N termini of ABP/ filamin, dystrophin, β-spectrin, and α-actinin.

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