Oligomerization, Membrane Anchoring, and Cellulose-binding Characteristics of AbpS, a Receptor-like Streptomyces Protein

Walter, Stefan; Schrempf, Hildgund

doi:10.1074/jbc.m212792200

Cited by 14 publications

(10 citation statements)

References 47 publications

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“…26. Proteins were incubated with Avicel PH-101 (Sigma, 11365) (1 mg/ml) in 20 mM Tris-Cl buffer, pH 8, and 150 mM NaCl for 120 min.…”

Section: Cobra Avicel and Cellohexaose Competition Assaymentioning

confidence: 99%

“…3). Avicel is a 95% pure crystalline cellulose with an average particle size of 50 m. Because Avicel is not soluble, competition assays with cellohexaose were carried out using pulldown assays (26). COBRA was incubated for 2 h at 21°C with Avicel in the presence of increasing concentrations of cellohexaose.…”

Section: Volume 289 • Number 50 • December 12 2014mentioning

confidence: 99%

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The Arabidopsis COBRA Protein Facilitates Cellulose Crystallization at the Plasma Membrane

Sorek

Kijac

et al. 2014

Journal of Biological Chemistry

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Background:The COBRA gene is highly coexpressed with cellulose synthase genes, but its function remains unclear. Results: COBRA localizes at the plasma membrane and binds glucan chains. NMR studies indicate structural defects in cellulose in the mutant despite normal polymerization rate. Conclusion: COBRA functions downstream of cellulose biosynthesis. Significance: This work suggests that alignment of glucan chains into cellulose fibrils is facilitated by one or more proteins.

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“…26. Proteins were incubated with Avicel PH-101 (Sigma, 11365) (1 mg/ml) in 20 mM Tris-Cl buffer, pH 8, and 150 mM NaCl for 120 min.…”

Section: Cobra Avicel and Cellohexaose Competition Assaymentioning

confidence: 99%

Section: Volume 289 • Number 50 • December 12 2014mentioning

confidence: 99%

The Arabidopsis COBRA Protein Facilitates Cellulose Crystallization at the Plasma Membrane

Sorek

Kijac

et al. 2014

Journal of Biological Chemistry

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“…The primary structure of both suggests a dimeric coiled coil; this and the previously-demonstrated tetramerisation of a FilP homologue, AbpS (Walter and Schrempf, 2003), are compatible with a mechanism of assembly not unlike that of intermediate filaments. However, in contrast to other bacterial cytoskeletal components such as CreS (Ausmees et al, 2003), the domain organisation and coiled-coil basis of Scy and FilP appears to be fundamentally distinct from that of IF and IF-like proteins.…”

Section: Discussionmentioning

confidence: 57%

“…The pairs in the top 6 rows represent intrahelical interactions, and those in the bottom 3 rows, inter-helical. dues 30-109; Walter and Schrempf, 2003). This suggests that at most one, and possibly neither, of the two domains alone possesses the ability to form the higher-order assemblies.…”

Section: The Scy and Filp Sequences Have Near-identical Domain Organimentioning

confidence: 95%

“…If the N-terminal canonical coiled coil of FilP forms a parallel arrangement, then possible g n to e n+1 pairings are Arg-Val, AspLeu, Arg-Glu, Arg-His, Glu-Gln and Gln-Glu , and three leucines at d. However, the notion that this combination appears even more classically dimer-like than Scy's, seems confounded by the demonstration that FilP's 93%-identical homologue in S. reticuli, known as AbpS, was shown to be tetrameric (Walter and Schrempf, 2003). However, the same authors showed that the progressive deletion of the N-terminus, including this coiled coil, resulted in the successive AbpS mutants becoming dimeric and unable to tetramerise.…”

Section: The Scy and Filp Sequences Have Near-identical Domain Organimentioning

confidence: 96%

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A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

Walshaw

Gillespie

Kelemen

2010

Journal of Structural Biology

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a b s t r a c tIn recent years, a number of bacterial coiled-coil proteins have been characterised which have roles in cell growth and morphology. Several have been shown to have a cytoskeletal function and some have been proposed to have an IF-like character in particular. We recently demonstrated in Streptomyces coelicolor a cytoskeletal role of Scy, a large protein implicated in filamentous growth, whose sequence is dominated by an unusual coiled-coil repeat. We present a detailed analysis of this 51-residue repeat and conclude that it is likely to form a parallel dimeric non-canonical coiled coil based on hendecads but with regions of local underwinding reflecting highly periodic modifications in the sequence. We also demonstrate that traditional sequence similarity searching is insufficient to identify all but the close orthologues of such repeat-dominated proteins, but that by an analysis of repeat periodicity and composition, remote homologues can be found. One clear candidate, despite a great size discrepancy and unremarkable sequence identity, is the known filament-former FilP in the same species. Both proteins appear distinct from the archetypal bacterial IF-like protein; they therefore may constitute a new class of bacterial filamentous protein. The similar sequence characteristics of both suggest their likely oligomer state and a possible mechanism for higher-order assembly into filaments. Another remote homologue in Actinomyces was highlighted by this method. Further, a known coiled-coil protein, DivIVA, appears to share some of these sequence characteristics.

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Intermediate Filaments Supporting Cell Shape and Growth in Bacteria

Kelemen

2017

Subcellular Biochemistry

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For years intermediate filaments (IF), belonging to the third class of filamentous cytoskeletal proteins alongside microtubules and actin filaments, were thought to be exclusive to metazoan cells. Structurally these eukaryote IFs are very well defined, consisting of globular head and tail domains, which flank the central rod-domain. This central domain is dominated by an α-helical secondary structure predisposed to form the characteristic coiled-coil, parallel homo-dimer. These elementary dimers can further associate, both laterally and longitudinally, generating a variety of filament-networks built from filaments in the range of 10 nm in diameter. The general role of these filaments with their characteristic mechano-elastic properties both in the cytoplasm and in the nucleus of eukaryote cells is to provide mechanical strength and a scaffold supporting diverse shapes and cellular functions.Since 2003, after the first bacterial IF-like protein, crescentin was identified, it has been evident that bacteria also employ filamentous networks, other than those built from bacterial tubulin or actin homologues, in order to support their cell shape, growth and, in some cases, division. Intriguingly, compared to their eukaryote counterparts, the group of bacterial IF-like proteins shows much wider structural diversity. The sizes of both the head and tail domains are markedly reduced and there is great variation in the length of the central rod-domain. Furthermore, bacterial rod-domains often lack the sub-domain organisation of eukaryote IFs that is the defining feature of the IF-family. However, the fascinating display of filamentous assemblies, including rope, striated cables and hexagonal laces together with the conditions required for their formation both in vitro and in vivo strongly resemble that of eukaryote IFs suggesting that these bacterial proteins are deservedly classified as part of the IF-family and that the current definition should be relaxed slightly to allow their inclusion. The lack of extensive head and tail domains may well make the bacterial proteins more amenable for structural characterisation, which will be essential for establishing the mechanism for their association into filaments. What is more, the well-developed tools for bacterial manipulations provide an excellent opportunity of studying the bacterial systems with the prospect of making significant progress in our understanding of the general underlying principles of intermediate filament assemblies.

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Oligomerization, Membrane Anchoring, and Cellulose-binding Characteristics of AbpS, a Receptor-like Streptomyces Protein

Cited by 14 publications

References 47 publications

The Arabidopsis COBRA Protein Facilitates Cellulose Crystallization at the Plasma Membrane

The Arabidopsis COBRA Protein Facilitates Cellulose Crystallization at the Plasma Membrane

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

Intermediate Filaments Supporting Cell Shape and Growth in Bacteria

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