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Titolo:
Impact of amino acids 22-27 of Rho-subfamily GTPases on glucosylation by the large clostridial cytotoxins TcsL-1522, TcdB-1470 and TcdB-8864
Autore:
Muller, S; von Eichel-Streiber, C; Moos, M;
Indirizzi:
Univ Mainz, Inst Med Mikrobiol & Hyg, Verfugungsgebaude Forsch & Entwicklung, D-55101 Mainz, Germany Univ Mainz Mainz Germany D-55101 h & Entwicklung, D-55101 Mainz, Germany
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 3, volume: 266, anno: 1999,
pagine: 1073 - 1080
SICI:
0014-2956(199912)266:3<1073:IOAA2O>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE EXCHANGE FACTORS; RESPIRATORY BURST OXIDASE; GTP-BINDING PROTEINS; STRUCTURAL BASIS; CRYSTAL-STRUCTURE; ACTIVATING-PROTEIN; EFFECTOR REGION; INSERT REGION; NADPH OXIDASE; TOXIN-B;
Keywords:
Clostridium difficile; Clostridium sordellii; glucosyltransferase; large clostridial cytotoxin; small GTP-binding proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: von Eichel-Streiber, C Univ Mainz, Inst Med Mikrobiol & Hyg, Verfugungsgebaude Forsch & Entwicklung, Obere Zahlbacherstr 63, D-55101 Mainz, Germany Univ Mainz Obere Zahlbacherstr 63 Mainz Germany D-55101
Citazione:
S. Muller et al., "Impact of amino acids 22-27 of Rho-subfamily GTPases on glucosylation by the large clostridial cytotoxins TcsL-1522, TcdB-1470 and TcdB-8864", EUR J BIOCH, 266(3), 1999, pp. 1073-1080

Abstract

Here we report data describing some principles of the interaction between small GTP-binding proteins and large Clostridial cytotoxins (LCTs). Our investigation was based on the differential glucosylation of Rac1 versus RhoA by LCTs TcsL-1522, TcdB-1470 and TcdB-8864. Chimeric RhoA/Rac1 proteins andGTPases mutated at defined regions or single amino acids were used as substrates. Starting with chimeric Rac/Rho proteins we demonstrated that proteins containing the N-terminal 73 amino acids of Rad (but not those of RhoA) were efficiently glucosylated. Within this stretch, three regions differ significantly in Rad and RhoA. Regions containing amino acids 41-45 and 50-54had no effect on toxin induced glucosylation, whereas amino acids 22-27 had a drastic impact on the potential of all three toxins to covalently modify the GTPases. Point mutations K25T of RhoA (numbering according to Rad) and K27A of Cdc42 significantly increased glucosylation by the cytotoxins; introduction of lysines at the equivalent positions of Rad hindered modification. Our experiments demonstrate the influence of this charged residue on GTPase-LCT interactions. Amino acids 22-27 are part of the transition between the alpha 1-helix to the switch I region of small GTP-binding proteins; both are known structures for specificity determination of the interactions with physiologic partners. Comparing these structures with data from our investigation we suggest that TcsL-1522, TcdB-1470 and TcdB-8864 mimic aspects of the physiologic interactions of small GTP-binding proteins.

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Documento generato il 07/08/20 alle ore 00:06:02