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Titolo:
"Lysine is the Lord", thought some scientists in regard to the group interacting with fluorescein isothiocyanate in ATP-binding sites of P-type ATPases - But, is it not cysteine?
Autore:
Breier, A; Ziegelhoffer, A;
Indirizzi:
Slovak Acad Sci, Inst Mol Physiol & Genet, Bratislava 83334, Slovakia Slovak Acad Sci Bratislava Slovakia 83334 et, Bratislava 83334, Slovakia Slovak Acad Sci, Heart Res Inst, Bratislava 84233, Slovakia Slovak Acad Sci Bratislava Slovakia 84233 st, Bratislava 84233, Slovakia
Titolo Testata:
GENERAL PHYSIOLOGY AND BIOPHYSICS
fascicolo: 3, volume: 19, anno: 2000,
pagine: 253 - 263
SICI:
0231-5882(200009)19:3<253:"ITLTS>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; CATION-TRANSPORT ATPASES; DEPENDENT PROTEASE-LA; MEMBRANE CA-2+ PUMP; ESCHERICHIA-COLI; SARCOPLASMIC-RETICULUM; SODIUM-PUMP; ACTIVE-SITE; LON GENE; SACCHAROMYCES-CEREVISIAE;
Keywords:
P-type ATPases; ATP dependent proteases; ATP-binding site; isothiocyanates; thiol and amino groups;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Breier, A Slovak Acad Sci, Inst Mol Physiol & Genet, Vlarska 5, Bratislava83334, Slovakia Slovak Acad Sci Vlarska 5 Bratislava Slovakia 83334 4, Slovakia
Citazione:
A. Breier e A. Ziegelhoffer, ""Lysine is the Lord", thought some scientists in regard to the group interacting with fluorescein isothiocyanate in ATP-binding sites of P-type ATPases - But, is it not cysteine?", GEN PHYSL B, 19(3), 2000, pp. 253-263

Abstract

Isothiocyanates are recognized inhibitors acting on ATP-binding sites of P-type ATPases. Detailed studies with modification of proteins in molecules of purified;ATPases by fluorescein isothiocyanate (FITC) and consequent tryptic hydrolysis followed by isolation and sequencing of the respective peptide fragments revealed FITC bound to a lysine residue. This residue was then indicated to be essential for the interaction of ATP with the P-type ATPases. Nevertheless, upon an exchange by site directed mutagenesis of lysine,believed to be essential, the expected total inhibition of ATPase activitywas missing. In addition, in the case of the plasma membrane Ca2+-ATPase, the residual activity still remained sensitive to FITC. It was attempted toexplain the latter finding by hypothetical existence of some other lysine residue essential for the ATPase activity. On the contrary, in our previousstudies we have shown that, based on the reactivity of isothiocyanates, the primary target of FITC in P-type ATPases has to be the SH group of a cysteine residue. However, later on, in altered conditions during trypsinolysisand sequencing, FITC may become transferred from its original site of interaction to a lysine residue and this may lead to final identification of the label on a false place. The present study represents an attempt of elucidating the controversy whether it is lysine or cysteine that represents the FITC-sensitive group truly responsible for the recognition by the active site of P-type ATPases of ATP and its binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:36:16