English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  p21 with a phenylalanine 28----leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties

Reinstein, J., Schlichting, I., Frech, M., Goody, R. S., & Wittinghofer, A. (1991). p21 with a phenylalanine 28----leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties. The Journal of Biological Chemistry, 266(26), 17700-17706. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/1894650.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-ACA5-D Version Permalink: http://hdl.handle.net/21.11116/0000-0002-69B8-9
Genre: Journal Article

Files

show Files
hide Files
:
JBiolChem_266_1991_17700.pdf (Any fulltext), 4MB
 
File Permalink:
-
Name:
JBiolChem_266_1991_17700.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Reinstein, Jochen1, Author              
Schlichting, Ilme1, Author              
Frech, Matthias, Author
Goody, Roger S.2, Author              
Wittinghofer, Alfred2, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: The H-ras gene product p21H has been mutated at Phe-28, which makes a hydrophobic interaction with the guanine base of bound GDP/GTP. The mutation Phe-28----Leu drastically increases nucleotide dissociation rates without affecting association rates. This is due to a perturbed binding of base, alpha- and beta-phosphate, and Mg2+, as evidenced from 31P NMR and fluorescence measurements. The region around the gamma-phosphate appears normal. The affinity of Mg2+ for both the di- and the triphosphate conformation of the mutant was also measured by fluorescence. The association constant is 3.5 x 10(7) M-1 for the Gpp(NH)p complex, 500 times higher than for the GDP form. The mutation does not change appreciably the intrinsic or the GTPase activating protein (GAP)-stimulated GTPase. The mutated protein induces neurite differentiation however when pressure-loaded into PC12 cells, which is equivalent to transformation of NIH 3T3 cells. This shows that p21 (F28L) is converted to the GDP bound form by GAP but is transforming because the high dissociation rate for nucleotides leads to a protein predominantly in the active GTP bound form.

Details

show
hide
Language(s): eng - English
 Dates: 1990-11-291991
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 266 (26) Sequence Number: - Start / End Page: 17700 - 17706 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1