2002
DOI: 10.1074/jbc.m109193200
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The Oligogalacturonate-specific Porin KdgM of Erwinia chrysanthemi Belongs to a New Porin Family

Abstract: The phytopathogenic Gram-negative bacteria Erwinia chrysanthemi secretes pectinases, which are able to degrade the pectic polymers of plant cell walls, and uses the degradation products as a carbon source for growth. We characterized a major outer membrane protein, KdgM, whose synthesis is strongly induced in the presence of pectic derivatives. The corresponding gene was characterized. Analysis of transcriptional fusions showed that the kdgM expression is controlled by the general repressor of pectinolytic gen… Show more

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Cited by 54 publications
(75 citation statements)
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References 64 publications
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“…Unlike KdgM, which can be closed only at positive potential, NanC exhibited voltage-dependent closure at both polarities. In the case of KdgM, which is involved in oligogalacturonide transport, we showed that trigalacturonate was able to induce fast blockade of the channel (3). No effect of Neu5Ac was observed in the experiments performed with NanC.…”
Section: Discussionmentioning
confidence: 71%
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“…Unlike KdgM, which can be closed only at positive potential, NanC exhibited voltage-dependent closure at both polarities. In the case of KdgM, which is involved in oligogalacturonide transport, we showed that trigalacturonate was able to induce fast blockade of the channel (3). No effect of Neu5Ac was observed in the experiments performed with NanC.…”
Section: Discussionmentioning
confidence: 71%
“…The identified or predicted substrates of the KdgM family members are oligogalacturonate, oligorhamnogalacturonate, alginate, and Neu5Ac (3,22). The common feature of these compounds is the presence on the sugars of an acidic function.…”
Section: Discussionmentioning
confidence: 99%
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“…V. vulnificus is predicted to deploy an extracellular PL9, a periplasmic HG binding protein (endoVvCBM32) and endoVvPL2, and an intracellular oligogalacturonte lyase (exoVvPL22). HG transport is facilitated through a KdgM-like anionic porin (40,41), and intracellular transport is predicted to be facilitated by a solute-binding protein and an ABC transporter that is distally located in the genome but under similar regulation (20). This pathway differs from what has been biochemically defined for Y. enterocolitica (Fig.…”
Section: Biological Significance and Evolution Of Hg Utilization Pathmentioning
confidence: 55%