Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain 1 1Edited by T. Richmond

Schubert, Wolf‐Dieter; Göbel, Gero; Diepholz, Meikel; Darji, Ayub; Kloer, Daniel P.; Hain, Torsten; Chakraborty, Trinad; Wehland, Jürgen; Domann, Eugen; Heinz, Dirk W.

doi:10.1006/jmbi.2001.4989

Cited by 109 publications

(113 citation statements)

References 55 publications

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“…Strikingly, a similar N-terminal amputation of fission yeast Sds22 confers a temperature-sensitive mitotic defect (6), which may also correlate with compromised binding to PP1. Possibly, the N terminus of Sds22 folds into an N-terminal LRR-cap, like the one observed in the structure of Internalin B, a prokaryotic LRR protein of the Sds22-like family (38). Deletion of such a shielding cap may induce a distortion of some of the LRRs to avoid exposure of the hydrophobic core of the LRR-superhelix.…”

Section: Discussionmentioning

confidence: 94%

“…While we have opted for a virtually untwisted sheet as observed in other eukaryotic proteins with Sds22-like LRRs and an LRR-cap, a modest right-handed twist of the sheet cannot be excluded. Such a twist occurs in the proteins Internalin B, which consists largely of Sds22-like LRRs (38), and YopM, which has shorter LRRs of the so-called bacterial class (42). The right-handed twist of these proteins has been tentatively explained by the repulsion of exposed negatively charged side-chains that occupy a fixed position in the second half of neighboring repeats (34).…”

Section: Discussionmentioning

confidence: 99%

“…The conformation, curvature, and twist of the ␤-sheet and of the turns around the asparagine-ladder, as well as the architecture of the attached LRR-cap is virtually identical in these eukaryotic proteins (35)(36)(37). The prokaryotic fourth protein with Sds22-like LRRs, Internalin B, lacks an LRR-cap and displays a slight right-handed twist of the otherwise similar concave surface of the superhelix (38).…”

Section: Glc-wtmentioning

confidence: 99%

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Binding of the Concave Surface of the Sds22 Superhelix to the α4/α5/α6-Triangle of Protein Phosphatase-1

Ceulemans

Vulsteke

Maeyer

et al. 2002

Journal of Biological Chemistry

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Functional studies of the protein phosphatase-1 (PP1) regulator Sds22 suggest that it is indirectly and/or directly involved in one of the most ancient functions of PP1, i.e. reversing phosphorylation by the Aurora-related protein kinases. We predict that the conserved portion of Sds22 folds into a curved superhelix and demonstrate that mutation to alanine of any of eight residues (Asp 148 Among the protein phosphatases that occur in all studied eukaryotic lineages, the Ser/Thr-specific protein phosphatases of type-1 are the best conserved, with more than 70% of their residues nearly invariant (1). This conservation extends well beyond structurally and catalytically important residues to include exposed residues involved in the binding of regulatory proteins. As a catalytic subunit, PP1 1 depends on the interaction with one or two regulatory subunits for subcellular localization, substrate specificity, and activity regulation (1, 2). Eukaryotic cells contain a large variety of regulatory subunits of PP1, which account for the diversified action of this phosphatase. We have recently proposed that PP1 acquired an essential function during early eukaryotic evolution by the development of sites for interaction with a primordial regulatory subunit(s) (1). This essential primordial function and the sequential acquirement of additional interaction sites and functions would then have impeded further mutation of the corresponding portion(s) of the surface. The phylogenetic distribution of PP1 indicates that this primordial function must have been acquired before the divergence of the extant eukaryotic lineages. One of the most ancient functions of PP1 is to dephosphorylate substrates of the Aurora-related protein kinases, and this is essential for the completion of mitosis (3). The regulatory subunit(s) associated with this function of PP1 remain unknown, but the protein Sds22 (38 kDa) has emerged as a prime candidate. First, both yeast and mammalian Sds22 have been shown to interact with PP1 and to be part of a complex with PP1 that is enriched in the nucleus (4 -7). Second, the Sds22 encoding gene was identified independently in fission and in budding yeast as an extra-copy suppressor of the temperaturesensitive mitotic arrest phenotypes that are associated with certain mutations of PP1 (4,5,8). Deletion of the Sds22-encoding gene caused a similar mitotic arrest, and this phenotype could be complemented by the overexpression of PP1 (4,5,8). Third, the conditionally lethal phenotype in budding yeast that was conferred by a loss-of-function mutation of the Aurora-related kinase Ipl1 (Ipl1-2), was largely relieved by the expression of certain temperature-sensitive mutant versions of Sds22 or PP1 (9, 10). The mutant Sds22 version that rescued the Ipl1-2 phenotype showed a decreased ability to interact with PP1. The expression of this mutant Sds22 did not affect the cellular levels of PP1 or Sds22, but drastically reduced the nuclear level of PP1 and caused a redistribution of the nuclear pool of PP1 (9).Hitherto, little ...

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Section: Glc-wtmentioning

confidence: 99%

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Binding of the Concave Surface of the Sds22 Superhelix to the α4/α5/α6-Triangle of Protein Phosphatase-1

Ceulemans

Vulsteke

Maeyer

et al. 2002

Journal of Biological Chemistry

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“…37 The crystal structures of the LRR and LRR/IR domains and full-length protein indicate that InlB has a highly elongated structure, suggesting an interaction with multiple cell receptors, that cooperate in bacterial uptake. [76][77][78] Indeed, various host receptors have been identified for InlB: gC1qR, c-Met and glycosaminoglycans (GAGs). A direct interaction between InlB and gC1qR has been shown.…”

Section: O N O T D I S T R I B U T Ementioning

confidence: 99%

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

et al. 2011

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“…When OD 600 reached 7.2 for the perdeuterated culture or 13.2 for the 50% deuterated culture, the temperature was decreased to 293K. GST-InlB 321 over-expression was induced by the addition of IPTG for 2h to reach a final concentration of 1 mM and incubation continued for 18 h. Cells were then harvested, washed with 10 mM HEPES (pH 6.4), and stored at 193 K. Purification of InlB 321 followed a published procedure 15 except that TEV protease was used to cleave the GST tag.…”

Section: -321 Of the Listeria Monocytogenes Inlb Gene Were Cloned Imentioning

confidence: 99%

X-ray and Neutron Small-Angle Scattering Analysis of the Complex Formed by the Met Receptor and the Listeria monocytogenes Invasion Protein InlB

Niemann

Petoukhov

Härtlein

et al. 2008

Journal of Molecular Biology

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Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain 1 1Edited by T. Richmond

Cited by 109 publications

References 55 publications

Binding of the Concave Surface of the Sds22 Superhelix to the α4/α5/α6-Triangle of Protein Phosphatase-1

Binding of the Concave Surface of the Sds22 Superhelix to the α4/α5/α6-Triangle of Protein Phosphatase-1

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

X-ray and Neutron Small-Angle Scattering Analysis of the Complex Formed by the Met Receptor and the Listeria monocytogenes Invasion Protein InlB

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