A role of disordered domains in regulating protein oligomerization and stability

Faust, Ofrah; Bigman, Lavi S.; Friedler, Assaf

doi:10.1039/c4cc03863k

Cited by 14 publications

(10 citation statements)

References 38 publications

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“…The reduced number of glutamic acid and lysine residues in the NTD, relative to that in the CTD (see table in Figure B), corresponded with the CTD being more disordered than that of the NTD. The identification of a highly disordered CTD domain along the FL sequence may explain the monomeric state of the protein, as previously demonstrated with other proteins …”

Section: Figuresupporting

confidence: 60%

The Bacterial Extracellular Matrix Protein TapA Is a Two‐Domain Partially Disordered Protein

et al. 2018

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Biofilms are aggregates of microbial cells that form on surfaces and at interfaces, and are encased in an extracellular matrix. In biofilms made by the soil bacterium Bacillus subtilis, the protein TapA mediates the assembly of the functional amyloid protein TasA into extracellular fibers, and it anchors these fibers to the cell surface. We used circular dichroism and NMR spectroscopy to show that, unlike the structured TasA, TapA is disordered. In addition, TapA is composed of two weakly interacting domains: a disordered C‐terminal domain and a more structured N‐terminal domain. These two domains also exhibited different structural changes in response to changes in external conditions, such as increased temperatures and the presence of lipid vesicles. Although the two TapA domains weakly interacted in solution, their cooperative interaction with lipid vesicles prevented disruption of the vesicles. These findings therefore suggest that the two‐domain composition of TapA is important in its interaction with single or multiple partners in the extracellular matrix in biofilms.

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Section: Figuresupporting

confidence: 60%

The Bacterial Extracellular Matrix Protein TapA Is a Two‐Domain Partially Disordered Protein

et al. 2018

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“…Although we had not previously found any indication of stabilization being achieved through direct intramolecular binding between the two Rev domains, [32] we do not exclude the possibility of long-distance,t ransient interactions. According to our current results, such interactions would be specifically www.chembiochem.org 2018 Wiley-VCH Verlag GmbH &Co. KGaA, Weinheim mediated by the 12 C-terminal residues of Rev.P erhaps the full-length C-terminal tail is important because it can function as af lexible linker,e nabling the 12 C-terminal residues to reach the structured domain and stay in its vicinity.T his means that an IDR can serve as al inker between as tructured domain and ad isordered subdomain, and not just between structured domains [34,35] as previously shown ( Figure 5A).…”

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confidence: 60%

“…[32,33] Circular dichroism( CD) spectroscopy showedt hat all of the deletion proteins showed two minima at 208 and 222 nm, indicative of an a-helical structure (Figure 1C). The NES between residues 74 and 83 was kept intact.…”

mentioning

confidence: 99%

Protein Regulation by Intrinsically Disordered Regions: A Role for Subdomains in the IDR of the HIV‐1 Rev Protein

et al. 2018

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Intrinsically disordered regions (IDRs) in proteins are highly abundant, but they are still commonly viewed as long stretches of polar, solvent-accessible residues. Here we show that the disordered C-terminal domain (CTD) of HIV-1 Rev has two subregions that carry out two distinct complementary roles of regulating protein oligomerization and contributing to stability. We propose that this takes place through a delicate balance between charged and hydrophobic residues within the IDR. This means that mutations in this region, as well as the known mutations in the structured region of the protein, can affect protein function. We suggest that IDRs in proteins should be divided into subdomains similarly to structured regions, rather than being viewed as long flexible stretches.

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“…1 ), a process described earlier to lead to homooligomeric proteins ( 39 ). As shown for several disordered proteins and domains ( 40 , 41 ), the CP12 domain is essential for hexamerization ( Fig. 2 ).…”

Section: Discussionmentioning

confidence: 71%

Structural and functional insights into the unique CBS–CP12 fusion protein family in cyanobacteria

Hackenberg

Hakanpää

Cai

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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SignificanceCarbon fixation is arguably one of the most important metabolic processes on Earth. Stand-alone CP12 proteins are major players in the regulation of this pathway in all oxygenic photosynthetic organisms, yet their intrinsic disorder has so far hampered the capturing of a principal part of their structure. Here we provide structural insights into CP12 by investigating an uncharacterized CP12 fusion protein, CBS–CP12, which is widespread among cyanobacteria, and reveal a unique hexameric structure. Our data further extend the existing knowledge of the regulation of photosynthesis and carbon fixation by the CP12 protein family, suggesting a more versatile role of this protein family in global redox regulation, predominantly in bloom-forming cyanobacteria that pose major threats in lakes and reservoirs.

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A role of disordered domains in regulating protein oligomerization and stability

Cited by 14 publications

References 38 publications

The Bacterial Extracellular Matrix Protein TapA Is a Two‐Domain Partially Disordered Protein

The Bacterial Extracellular Matrix Protein TapA Is a Two‐Domain Partially Disordered Protein

Protein Regulation by Intrinsically Disordered Regions: A Role for Subdomains in the IDR of the HIV‐1 Rev Protein

Structural and functional insights into the unique CBS–CP12 fusion protein family in cyanobacteria

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