ArticleJournal of bacteriology2009
Characterization of Streptococcus gordonii SecA2 as a paralogue of SecA.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- Mutations that confer resistance to sodium azide affect the levels of two physiological isoforms of SecA inMicrobiology (Reading, England) · 2026Article
- The Two Distinct Types of SecA2-Dependent Export Systems.Microbiology spectrum · 2019Review
- Membrane trafficking of the bacterial adhesin GspB and the accessory Sec transport machinery.The Journal of biological chemistry · 2019Article
- Streptococcus endopeptidases promote HPV infection in vitro.MicrobiologyOpen · 2019Article
- O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport.PLoS pathogens · 2017Article
- A prl mutation in SecY suppresses secretion and virulence defects of Listeria monocytogenes secA2 mutants.Journal of bacteriology · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Selective transport by SecA2: an expanding family of customized motor proteins.Biochimica et biophysica acta · 2014Review
- Suppressor analysis reveals a role for SecY in the SecA2-dependent protein export pathway of Mycobacteria.Journal of bacteriology · 2013Article
- Differential localization of the streptococcal accessory sec components and implications for substrate export.Journal of bacteriology · 2013Article
- Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012Review
- The accessory Sec protein Asp2 modulates GlcNAc deposition onto the serine-rich repeat glycoprotein GspB.Journal of bacteriology · 2012Article
- A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis.Molecular oral microbiology · 2012Review
- A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec system.The Journal of biological chemistry · 2012Article
- Canonical SecA associates with an accessory secretory protein complex involved in biogenesis of a streptococcal serine-rich repeat glycoprotein.Journal of bacteriology · 2011Article
- Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec System.Journal of bacteriology · 2011Article
- The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri.PLoS genetics · 2011Article
- Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii.Molecular microbiology · 2010Article
- Transport of preproteins by the accessory Sec system requires a specific domain adjacent to the signal peptide.Journal of bacteriology · 2010Article
- Protein transport across and into cell membranes in bacteria and archaea.Cellular and molecular life sciences : CMLS · 2010Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The accessory Sec system of Streptococcus gordonii is essential for transport of the glycoprotein GspB to the bacterial cell surface. A key component of this dedicated transport system is SecA2. The SecA2 proteins of streptococci and staphylococci are paralogues of SecA and are presumed to have an analogous role in protein transport, but they may be specifically adapted for the transport of large, serine-rich glycoproteins. We used a combination of genetic and biochemical methods to assess whether the S. gordonii SecA2 functions similarly to SecA. Although mutational analyses demonstrated that conserved amino acids are essential for the function of SecA2, replacing such residues in one of two nucleotide binding folds had only minor effects on SecA2 function. SecA2-mediated transport is highly sensitive to azide, as is SecA-mediated transport. Comparison of the S. gordonii SecA and SecA2 proteins in vitro revealed that SecA2 can hydrolyze ATP at a rate similar to that of SecA and is comparably sensitive to azide but that the biochemical properties of these enzymes are subtly different. That is, SecA2 has a lower solubility in aqueous solutions and requires higher Mg(2+) concentrations for maximal activity. In spite of the high degree of similarity between the S. gordonii paralogues, analysis of SecA-SecA2 chimeras indicates that the domains are not readily interchangeable. This suggests that specific, unique contacts between SecA2 and other components of the accessory Sec system may preclude cross-functioning with the canonical Sec system.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.