Document Detail

Site-directed mutations altering methyl-accepting residues of a sensory transducer protein.
MedLine Citation:
PMID:  3041407     Owner:  NLM     Status:  MEDLINE    
The Trg protein is one of a family of transducer proteins that mediate chemotactic response in Escherichia coli. Transducers are methyl-accepting proteins that gain or lose methyl esters on specific glutamyl residues during sensory adaptation. In this study, the significance of multiple sites of methylation on transducer proteins was addressed by using oligonucleotide-directed, site-specific mutagenesis to substitute an alanyl residue at each of the five methyl-accepting sites in Trg. The resulting collection of five mutations, each inactivating a single site, was analyzed for effects on covalent modification at the remaining sites on Trg and for the ability of the altered proteins to mediate sensory adaptation. Most of the alanyl substitutions had substantial biochemical effects, enhancing or reducing methyl-accepting activity of other sites, including one case of activation of a site not methylated in wild-type protein. Analysis of the altered proteins provided explanations for many features of the complex pattern of electrophoretic forms exhibited by Trg. The mutant proteins were less efficient than normal Trg in mediating adaptation. Correlation of biochemical and behavioral data indicated that reduction in the number of methyl-accepting sites on the transducer lengthened the time required to reach an adapted state.
D M Nowlin; J Bollinger; G L Hazelbauer
Related Documents :
4041467 - Physical properties of chicken erythrocyte hmg-1, hmg-2 and hmg-e.
17728347 - The first bromodomain of brdt, a testis-specific member of the bet sub-family of double...
14603467 - Oligodendrocyte process outgrowth in vitro is modulated by epigenetic regulation of cyt...
1715527 - Exogenous gangliosides may affect methylation mechanisms in neuronal cell cultures.
25369867 - Quantitative proteomic analysis of down syndrome in the umbilical cord blood using itraq.
20496947 - Vinyl sulfone bifunctional tag reagents for single-point modification of proteins.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proteins     Volume:  3     ISSN:  0887-3585     ISO Abbreviation:  Proteins     Publication Date:  1988  
Date Detail:
Created Date:  1988-08-26     Completed Date:  1988-08-26     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  102-12     Citation Subset:  IM    
Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
Bacterial Proteins / genetics*
Escherichia coli / genetics*,  physiology
Escherichia coli Proteins*
Membrane Proteins
Molecular Sequence Data
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Membrane Proteins; 0/Trg protein, E coli; 56-41-7/Alanine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Regulatory aspects of placental iron transfer--a comparative study.
Next Document:  Discrete-time random walks on diagrams (graphs) with cycles.