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Complete genome and proteome of Acholeplasma laidlawii.

Authors :
Lazarev VN
Levitskii SA
Basovskii YI
Chukin MM
Akopian TA
Vereshchagin VV
Kostrjukova ES
Kovaleva GY
Kazanov MD
Malko DB
Vitreschak AG
Sernova NV
Gelfand MS
Demina IA
Serebryakova MV
Galyamina MA
Vtyurin NN
Rogov SI
Alexeev DG
Ladygina VG
Govorun VM
Source :
Journal of bacteriology [J Bacteriol] 2011 Sep; Vol. 193 (18), pp. 4943-53. Date of Electronic Publication: 2011 Jul 22.
Publication Year :
2011

Abstract

We present the complete genome sequence and proteogenomic map for Acholeplasma laidlawii PG-8A (class Mollicutes, order Acholeplasmatales, family Acholeplasmataceae). The genome of A. laidlawii is represented by a single 1,496,992-bp circular chromosome with an average G+C content of 31 mol%. This is the longest genome among the Mollicutes with a known nucleotide sequence. It contains genes of polymerase type I, SOS response, and signal transduction systems, as well as RNA regulatory elements, riboswitches, and T boxes. This demonstrates a significant capability for the regulation of gene expression and mutagenic response to stress. Acholeplasma laidlawii and phytoplasmas are the only Mollicutes known to use the universal genetic code, in which UGA is a stop codon. Within the Mollicutes group, only the sterol-nonrequiring Acholeplasma has the capacity to synthesize saturated fatty acids de novo. Proteomic data were used in the primary annotation of the genome, validating expression of many predicted proteins. We also detected posttranslational modifications of A. laidlawii proteins: phosphorylation and acylation. Seventy-four candidate phosphorylated proteins were found: 16 candidates are proteins unique to A. laidlawii, and 11 of them are surface-anchored or integral membrane proteins, which implies the presence of active signaling pathways. Among 20 acylated proteins, 14 contained palmitic chains, and six contained stearic chains. No residue of linoleic or oleic acid was observed. Acylated proteins were components of mainly sugar and inorganic ion transport systems and were surface-anchored proteins with unknown functions.<br /> (Copyright © 2011, American Society for Microbiology. All Rights Reserved.)

Details

Language :
English
ISSN :
1098-5530
Volume :
193
Issue :
18
Database :
MEDLINE
Journal :
Journal of bacteriology
Publication Type :
Academic Journal
Accession number :
21784942
Full Text :
https://doi.org/10.1128/JB.05059-11