Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain

S. Yu Khaitlina, J. H. Collins, I. M. Kuznetsova, V. P. Pershina, Irina Sinakevitch, K. K. Turoverov, A. M. Usmanova

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain [(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal amino acid residues of the parent molecule. The E. coli protease split actin preserves the NH2-terminal part of the polypeptide chain as well as the native conformation of actin molecule. However, the E. coli protease split actin failed to polymerize in 0.1 M KCl, suggesting that integrity of actin molecule between Gly-42 and Val-43 is crucial for actin polymerization.

Original languageEnglish (US)
Pages (from-to)49-51
Number of pages3
JournalFEBS Letters
Volume279
Issue number1
DOIs
StatePublished - Feb 11 1991
Externally publishedYes

Fingerprint

varespladib methyl
Chemical properties
Escherichia coli
Actins
Molecules
Peptide Hydrolases
Polymerization
Conformations
protease E
Amino Acids
Peptides

Keywords

  • Bacterial protease
  • Intrinsic fluoroscence
  • Split actin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Khaitlina, S. Y., Collins, J. H., Kuznetsova, I. M., Pershina, V. P., Sinakevitch, I., Turoverov, K. K., & Usmanova, A. M. (1991). Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain. FEBS Letters, 279(1), 49-51. https://doi.org/10.1016/0014-5793(91)80247-Z

Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain. / Khaitlina, S. Yu; Collins, J. H.; Kuznetsova, I. M.; Pershina, V. P.; Sinakevitch, Irina; Turoverov, K. K.; Usmanova, A. M.

In: FEBS Letters, Vol. 279, No. 1, 11.02.1991, p. 49-51.

Research output: Contribution to journalArticle

Khaitlina, SY, Collins, JH, Kuznetsova, IM, Pershina, VP, Sinakevitch, I, Turoverov, KK & Usmanova, AM 1991, 'Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain', FEBS Letters, vol. 279, no. 1, pp. 49-51. https://doi.org/10.1016/0014-5793(91)80247-Z
Khaitlina SY, Collins JH, Kuznetsova IM, Pershina VP, Sinakevitch I, Turoverov KK et al. Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain. FEBS Letters. 1991 Feb 11;279(1):49-51. https://doi.org/10.1016/0014-5793(91)80247-Z
Khaitlina, S. Yu ; Collins, J. H. ; Kuznetsova, I. M. ; Pershina, V. P. ; Sinakevitch, Irina ; Turoverov, K. K. ; Usmanova, A. M. / Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain. In: FEBS Letters. 1991 ; Vol. 279, No. 1. pp. 49-51.
@article{ba7aab268d59418bb94b1f8e04cb94ed,
title = "Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain",
abstract = "The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain [(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal amino acid residues of the parent molecule. The E. coli protease split actin preserves the NH2-terminal part of the polypeptide chain as well as the native conformation of actin molecule. However, the E. coli protease split actin failed to polymerize in 0.1 M KCl, suggesting that integrity of actin molecule between Gly-42 and Val-43 is crucial for actin polymerization.",
keywords = "Bacterial protease, Intrinsic fluoroscence, Split actin",
author = "Khaitlina, {S. Yu} and Collins, {J. H.} and Kuznetsova, {I. M.} and Pershina, {V. P.} and Irina Sinakevitch and Turoverov, {K. K.} and Usmanova, {A. M.}",
year = "1991",
month = "2",
day = "11",
doi = "10.1016/0014-5793(91)80247-Z",
language = "English (US)",
volume = "279",
pages = "49--51",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Physico-chemical properties of actin cleaved with bacterial protease from E. coli A2 strain

AU - Khaitlina, S. Yu

AU - Collins, J. H.

AU - Kuznetsova, I. M.

AU - Pershina, V. P.

AU - Sinakevitch, Irina

AU - Turoverov, K. K.

AU - Usmanova, A. M.

PY - 1991/2/11

Y1 - 1991/2/11

N2 - The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain [(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal amino acid residues of the parent molecule. The E. coli protease split actin preserves the NH2-terminal part of the polypeptide chain as well as the native conformation of actin molecule. However, the E. coli protease split actin failed to polymerize in 0.1 M KCl, suggesting that integrity of actin molecule between Gly-42 and Val-43 is crucial for actin polymerization.

AB - The 36 kDa fragment of actin molecule obtained with the protease from E. coli A2 strain [(1988) FEBS Lett. 228, 172] was shown to begin with Val-43 and retain the COOH-terminal amino acid residues of the parent molecule. The E. coli protease split actin preserves the NH2-terminal part of the polypeptide chain as well as the native conformation of actin molecule. However, the E. coli protease split actin failed to polymerize in 0.1 M KCl, suggesting that integrity of actin molecule between Gly-42 and Val-43 is crucial for actin polymerization.

KW - Bacterial protease

KW - Intrinsic fluoroscence

KW - Split actin

UR - http://www.scopus.com/inward/record.url?scp=0026079005&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026079005&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(91)80247-Z

DO - 10.1016/0014-5793(91)80247-Z

M3 - Article

VL - 279

SP - 49

EP - 51

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -