Literature DB >> 3014969

Location of the guanosine triphosphate (GTP) hydrolysis site in microtubules.

M Caplow.   

Abstract

The rate for GTP hydrolysis remains approximately constant during microtubule assembly from microtubular protein. This indicates that GTP hydrolysis does not accompany tubulin-GTP subunit addition to microtubule ends. We suggest that GTP, within tubulin-GTP subunits that are incorporated into microtubules, is hydrolyzed predominantly at one or both microtubule ends at an interface of a cap of tubulin-GTP subunits and a core of tubulin-GDP subunits.

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Year:  1986        PMID: 3014969     DOI: 10.1111/j.1749-6632.1986.tb38428.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  3 in total

1.  Kinetics of GTP hydrolysis during the assembly of chick brain MAP2-tubulin microtubule protein.

Authors:  R G Burns
Journal:  Biochem J       Date:  1991-07-01       Impact factor: 3.857

2.  Assembly of chick brain MAP2-tubulin microtubule protein. Analysis of tubulin subunit flux rates by immunofluorescence microscopy.

Authors:  M F Symmons; R G Burns
Journal:  Biochem J       Date:  1991-07-01       Impact factor: 3.857

3.  Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies.

Authors:  R A Walker; E T O'Brien; N K Pryer; M F Soboeiro; W A Voter; H P Erickson; E D Salmon
Journal:  J Cell Biol       Date:  1988-10       Impact factor: 10.539

  3 in total

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