Literature DB >> 2506852

cDNA cloning of Gb, the substrate for botulinum ADP-ribosyltransferase from bovine adrenal gland and its identification as a rho gene product.

T Ogorochi1, Y Nemoto, M Nakajima, E Nakamura, M Fujiwara, S Narumiya.   

Abstract

A 1.5 kilobase cDNA coding for the complete amino acid sequence of Gb, the substrate for ADP-ribosyltransferase in C1 and D botulinum toxins from bovine adrenal gland, has been isolated from a cDNA library of bovine adrenal gland. This cDNA encodes a polypeptide of 21,770 Da consisting of 193 amino acid residues, and the deduced amino acid sequence contains all the partial amino acid sequences reported previously (Narumiya, S., Sekine, A., and Fujiwara, M. (1988) J. Biol. Chem., 263, 17255-17257). Sequence comparison revealed that Gb is identical with the product of human rho clone 12 (rho A). The present results also confirmed our suggestion that the ADP-ribosylation occurs at Asn41 in the putative effector domain of the rho gene product.

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Year:  1989        PMID: 2506852     DOI: 10.1016/0006-291x(89)92344-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  ADP-ribosylation of the GTP-binding protein RhoA blocks cytoplasmic division in human myelomonocytic cells.

Authors:  M Aepfelbacher; M Essler; K Luber De Quintana; P C Weber
Journal:  Biochem J       Date:  1995-06-15       Impact factor: 3.857

2.  Stimulation of phospholipase C-beta2 by the Rho GTPases Cdc42Hs and Rac1.

Authors:  D Illenberger; F Schwald; D Pimmer; W Binder; G Maier; A Dietrich; P Gierschik
Journal:  EMBO J       Date:  1998-11-02       Impact factor: 11.598

3.  Bacterial ADP-ribosyltransferase with a substrate specificity of the rho protein disassembles the Golgi apparatus in Vero cells and mimics the action of brefeldin A.

Authors:  M Sugai; C H Chen; H C Wu
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-01       Impact factor: 11.205

  3 in total

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