Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Published online ahead of print on 1 October 2009 as doi:10.1099/mic.0.033480-0
Microbiology (2009), DOI 10.1099/mic.0.033480-0
© 2009 Society for General Microbiology
This Article
Right arrow Full Text (Papers in Press[PDF])
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Google Scholar
Right arrow Articles by Dávila-Martínez, Y.
Right arrow Articles by López-Lara, I. M.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dávila-Martínez, Y.
Right arrow Articles by López-Lara, I. M.
Agricola
Right arrow Articles by Dávila-Martínez, Y.
Right arrow Articles by López-Lara, I. M.
Microbiology 0 (2009), mic.0.033480; DOI  10.1099/mic.0.033480-0
© 2009 Society for General Microbiology

SMc01553 is the sixth acyl carrier protein in Sinorhizobium meliloti 1021

Yadira Dávila-Martínez, Ana Laura Ramos-Vega, Sandra Contreras-Martínez, Sergio Encarnación, Otto Geiger and Isabel M. López-Lara1

Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México

Acyl carrier proteins (ACPs) are required for the transfer of acyl intermediates during fatty acid and polyketide syntheses. In Sinorhizobium meliloti 1021 there are 5 known ACPs: AcpP, NodF, AcpXL, the ACP domain in RkpA and SMb20651. The genome sequence of S. meliloti 1021 also reveals the ORF SMc01553 annotated as putative ACP. Gene smc01553 is part of a 6.6 kb DNA region that is duplicated in the chromosome and in the pSymb plasmid which is the result of a recent duplication event. SMc01553 overexpressed in E. coli was labelled in vivo with [3H]β-alanine, a biosynthetic building block of the 4'-phosphopantetheine prosthetic group of ACPs. The purified SMc01553 was modified with 4'-phosphopantetheine in the presence of S. meliloti holo-ACP synthase and this modification resulted in a major conformational change of the protein structure, since the holo-form runs faster in native PAGE than the apo-form. SMc01553 could not be loaded with a malonyl group by malonyl CoA-ACP transacylase from S. meliloti. Using RT-PCR we could show the presence of mRNA for SMc01553 and of the duplicated ORF SMb22007 in cultures of S. meliloti. However, a mutant in which the two duplicated regions were deleted did not show any different phenotype with respect to the wild type in the free-living or symbiotic life style.

1 E-mail: isabel{at}ccg.unam.mx






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2009 Society for General Microbiology.