Literature DB >> 3306924

Evidence for dispensable sequences inserted into a nucleotide fold.

R M Starzyk, T A Webster, P Schimmel.   

Abstract

Previous experimental results along with the structural modeling presented indicate that a nucleotide fold starts in the amino-terminal part of Escherichia coli isoleucyl-transfer RNA synthetase, a single chain polypeptide of 939 amino acids. Internal deletions were created in the region of the nucleotide fold. A set of deletions that collectively span 145 contiguous amino acids yielded active enzymes. Further extensions of the deletions yielded inactive or unstable proteins. The three-dimensional structure of an evidently homologous protein suggests that the active deletions lack portions of a segment that connects two parts of the nucleotide fold. Therefore, the results imply that removal of major sections of the polypeptide that connects these two parts of the fold does not result in major perturbation of the nucleotide binding site.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3306924     DOI: 10.1126/science.3306924

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  45 in total

1.  Domain-domain communication in a miniature archaebacterial tRNA synthetase.

Authors:  B A Steer; P Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  1999-11-23       Impact factor: 11.205

2.  Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase.

Authors:  Anthony C Bishop; Kirk Beebe; Paul R Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  2003-01-06       Impact factor: 11.205

3.  RNA binding determinant in some class I tRNA synthetases identified by alignment-guided mutagenesis.

Authors:  A Shepard; K Shiba; P Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-15       Impact factor: 11.205

4.  Functional assembly of a randomly cleaved protein.

Authors:  K Shiba; P Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  1992-03-01       Impact factor: 11.205

5.  Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps.

Authors:  Nevena Cvetesic; John J Perona; Ita Gruic-Sovulj
Journal:  J Biol Chem       Date:  2012-05-30       Impact factor: 5.157

6.  Inhibited cell growth and protein functional changes from an editing-defective tRNA synthetase.

Authors:  Jamie M Bacher; Valérie de Crécy-Lagard; Paul R Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  2005-01-12       Impact factor: 11.205

7.  Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity.

Authors:  Amy M Williams; Susan A Martinis
Journal:  Proc Natl Acad Sci U S A       Date:  2006-02-27       Impact factor: 11.205

8.  A unique insert of leucyl-tRNA synthetase is required for aminoacylation and not amino acid editing.

Authors:  Michael T Vu; Susan A Martinis
Journal:  Biochemistry       Date:  2007-04-04       Impact factor: 3.162

9.  Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity.

Authors:  Aswini K Betha; Amy M Williams; Susan A Martinis
Journal:  Biochemistry       Date:  2007-05-03       Impact factor: 3.162

10.  A domain for editing by an archaebacterial tRNA synthetase.

Authors:  Kirk Beebe; Eve Merriman; Lluis Ribas De Pouplana; Paul Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  2004-04-12       Impact factor: 11.205

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.