SMc01553 is the sixth acyl carrier protein in Sinorhizobium meliloti 1021

Dávila-Martínez, Yadira; Ramos-Vega, Ana Laura; Contreras-Martínez, Sandra; Encarnación, Sergio; Geiger, Otto; López‐Lara, Isabel M.

doi:10.1099/mic.0.033480-0

Cited by 9 publications

(12 citation statements)

References 42 publications

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“…ACPs play a crucial role in the assembly of the bacterial cell envelope and have been shown to play an important role in establishing a successful symbiosis (Geiger & López‐Lara, ). Currently, six ACPs have been identified and their functions confirmed in S. meliloti (Geiger & López‐Lara, ; Ramos‐Vega et al ., ; Davila‐Martinez et al ., ). A particular ACP is NodF, which is involved in the decoration of the Nod factor with a specific polyunsaturated fatty acid requiring also the NodE protein for its synthesis.…”

Section: Biosynthesis and Importance Of Unusual S Meliloti Lps Lipidsmentioning

confidence: 97%

Molecular insights into bacteroid development duringRhizobium–legume symbiosis

Haag¹,

Arnold²,

Myka³

et al. 2013

FEMS Microbiol Rev

111

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Rhizobial soil bacteria can form a symbiosis with legumes in which the bacteria fix atmospheric nitrogen into ammonia that can be utilized by the host. The plant, in turn, supplies the rhizobia with a carbon source. After infecting the host cell, the bacteria differentiate into a distinct bacteroid form, which is able to fix nitrogen. The bacterial BacA protein is essential for bacteroid differentiation in legumes producing nodule-specific cysteine-rich peptides (NCRs), which induce the terminal differentiation of the bacteria into bacteroids. NCRs are antimicrobial peptides similar to mammalian defensins, which are important for the eukaryotic response to invading pathogens. The BacA protein is essential for rhizobia to survive the NCR peptide challenge. Similarities in the lifestyle of intracellular pathogenic bacteria suggest that host factors might also be important for inducing chronic infections associated with Brucella abortus and Mycobacterium tuberculosis. Moreover, rhizobial lipopolysaccharide is modified with an unusual fatty acid, which plays an important role in protecting the bacteria from environmental stresses. Mutants defective in the biosynthesis of this fatty acid display bacteroid development defects within the nodule. In this review, we will focus on these key components, which affect rhizobial bacteroid development and survival.

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Section: Biosynthesis and Importance Of Unusual S Meliloti Lps Lipidsmentioning

confidence: 97%

Molecular insights into bacteroid development duringRhizobium–legume symbiosis

Haag¹,

Arnold²,

Myka³

et al. 2013

FEMS Microbiol Rev

111

View full text Add to dashboard Cite

show abstract

“…264 These presumably require a PPant arm for activity, show very little sequence identity (Fig. 18), and are modified by its endogenous AcpS.…”

Section: Carrier Protein(s)mentioning

confidence: 99%

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

et al. 2014

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Although holo-acyl carrier protein synthase, AcpS, a phosphopantetheinyl transferase (PPTase), was characterized in the 1960s, it was not until the publication of the landmark paper by Lambalot et al. in 1996 that PPTases garnered wide-spread attention being classified as a distinct enzyme superfamily. In the past two decades an increasing number of papers has been published on PPTases ranging from identification, characterization, structure determination, mutagenesis, inhibition, and engineering in synthetic biology. In this review, we comprehensively discuss all current knowledge on this class of enzymes that post-translationally install a 4′-phosphopantetheine arm on various carrier proteins.

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“…Sinorhizobium meliloti has at least six ACPs, and four of them have been well characterized ( Geiger and Lopez-Lara, 2002 ): AcpP for general fatty acid synthesis ( López-Lara and Geiger, 2000 ), NodF for the synthesis of polyunsaturated fatty acids in nodulation factors ( Demont et al, 1993 ; Demont-Caulet et al, 1999 ), AcpXL for the synthesis and transfer of 27-hydroxyoctacosanoic acid during rhizobial lipid A synthesis ( Brozek et al, 1996 ; Haag et al, 2011 ), and RkpF, which participates in the synthesis of rhizobial capsular polysaccharides ( Epple et al, 1998 ). The remaining two ACP homologs, SMc01553 and SMb20651, also have been identified as ACP-like proteins, but their functions need further investigation ( Ramos-Vega et al, 2009 ; Davila-Martinez et al, 2010 ).…”

Section: Introductionmentioning

confidence: 99%

Only Acyl Carrier Protein 1 (AcpP1) Functions in Pseudomonas aeruginosa Fatty Acid Synthesis

Cao³

et al. 2017

Front. Microbiol.

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The genome of Pseudomonas aeruginosa contains three open reading frames, PA2966, PA1869, and PA3334, which encode putative acyl carrier proteins, AcpP1, AcpP2, and AcpP3, respectively. In this study, we found that, although these apo-ACPs were successfully phosphopantetheinylated by P. aeruginosa phosphopantetheinyl transferase (PcpS) and all holo-forms of these proteins could be acylated by Vibrio harveyi acyl-ACP synthetase (AasS), only AcpP1 could be used as a substrate for the synthesis of fatty acids, catalyzed by P. aeruginosa cell free extracts in vitro, and only acpP1 gene could restore growth in the Escherichia coli acpP mutant strain CY1877. And P. aeruginosa acpP1 could not be deleted, while disruption of acpP2 or acpP3 in the P. aeruginosa genome allowed mutant strains to grow as well as the wild type strain. These findings confirmed that only P. aeruginosa AcpP1 functions in fatty acid biosynthesis, and that acpP2 and acpP3 do not play roles in the fatty acid synthetic pathway. Moreover, disruption of acpP2 and acpP3 did not affect the ability of P. aeruginosa to produce N-acylhomoserine lactones (AHL), but replacement of P. aeruginosa acpP1 with E. coli acpP caused P. aeruginosa to reduce the production of AHL molecules, which indicated that neither P. aeruginosa AcpP2 nor AcpP3 can act as a substrate for synthesis of AHL molecules in vivo. Furthermore, replacement of acpP1 with E. coli acpP reduced the ability of P. aeruginosa to produce some exo-products and abolished swarming motility in P. aeruginosa.

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SMc01553 is the sixth acyl carrier protein in Sinorhizobium meliloti 1021

Cited by 9 publications

References 42 publications

Molecular insights into bacteroid development duringRhizobium–legume symbiosis

Molecular insights into bacteroid development duringRhizobium–legume symbiosis

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

Only Acyl Carrier Protein 1 (AcpP1) Functions in Pseudomonas aeruginosa Fatty Acid Synthesis

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