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Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail

ABSTRACT: Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail

PROVIDER: PRJNA1013251 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25918900.fastq.gz	Fastqsanger.gz
	SRR25918901.fastq.gz	Fastqsanger.gz
	SRR25918888.fastq.gz	Fastqsanger.gz
	SRR25918889.fastq.gz	Fastqsanger.gz
	SRR25918890.fastq.gz	Fastqsanger.gz

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Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail

Project description:Cofilin family proteins have essential roles in remodeling the cytoskeleton through filamentous actin depolymerization and severing. The short unstructured N-terminal region of cofilin is critical for actin binding and harbors the major site of inhibitory phosphorylation. Atypically for a disordered sequence, the N-terminal region is highly conserved, but specifics aspects driving this conservation are unclear. Here, we screened a library of 16,000 human cofilin N-terminal sequence variants for their capacity to support growth in S. cerevisiae in the presence or absence of the upstream regulator LIM kinase. Results from the screen and biochemical analysis of individual variants revealed distinct sequence requirements for actin binding and regulation by LIM kinase. LIM kinase recognition only partly explained sequence constraints on phosphoregulation, which were instead driven to a large extent by the capacity for phosphorylation to inactivate cofilin. We found remarkably loose sequence requirements for actin binding and phosphoinhibition, but collectively they restricted the N-terminus to sequences found in natural cofilins. Our results illustrate how a phosphorylation site can balance potentially competing sequence requirements for function and regulation.

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Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail

Project description: Not available

| S-EPMC10873347 | biostudies-literature

Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail.

Project description:Cofilin family proteins have essential roles in remodeling the cytoskeleton through filamentous actin depolymerization and severing. The short unstructured N-terminal region of cofilin is critical for actin binding and harbors the major site of inhibitory phosphorylation. Atypically for a disordered sequence, the N-terminal region is highly conserved, but the aspects of cofilin functionality driving this conservation are not clear. Here, we screened a library of 16,000 human cofilin N-terminal sequence variants for their capacity to support growth in S. cerevisiae in the presence or absence of the upstream regulator LIM kinase. Results from the screen and subsequent biochemical analysis of individual variants revealed distinct sequence requirements for actin binding and regulation by LIM kinase. While the presence of a serine, rather than threonine, phosphoacceptor residue was essential for phosphorylation by LIM kinase, the native cofilin N-terminus was otherwise a suboptimal LIM kinase substrate. This circumstance was not due to sequence requirements for actin binding and severing, but rather appeared primarily to maintain the capacity for phosphorylation to inactivate cofilin. Overall, the individual sequence requirements for cofilin function and regulation were remarkably loose when examined separately, but collectively restricted the N-terminus to sequences found in natural cofilins. Our results illustrate how a regulatory phosphorylation site can balance potentially competing sequence requirements for function and regulation.

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Replacement of Arabidopsis H2A.Z with human H2A.Z orthologs reveals extensive functional conservation and limited importance of the N-terminal tail sequence for Arabidopsis development (ChIP-Seq)

Project description:To investigate the functional conservation of H2A.Z histones during eukaryotic evolution we transformed h2a.z deficient plants with three human H2A.Z proteins to assess their ability to rescue the mutant defects. We discovered that human H2A.Z.1 and H2A.Z.2.1 fully complement the phenotypic abnormalities of h2a.z plants even though Arabidopsis and human H2A.Z N-terminal tail sequences are divergent, while the brain-specific splice variant H2A.Z.2.2 has a dominant-negative effect in wild-type plants. Furthermore, H2A.Z.1 almost completely re-establishes normal H2A.Z chromatin occupancy in h2a.z plants and restores the expression of more than 84 % of misexpressed genes. Finally, our hypothesis that the N-terminal tail of Arabidopsis H2A.Z is not crucial for its overall function was supported by the ability of N-terminal end truncations of Arabidopsis HTA11 to largely rescue the defects of h2a.z mutants.

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Replacement of Arabidopsis H2A.Z with human H2A.Z orthologs reveals extensive functional conservation and limited importance of the N-terminal tail sequence for Arabidopsis development (WT, h2a.z + HsH2A.Z. RNA-Seq)

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2024-05-13 | GSE263310 | GEO

Histone H4 N-terminal tail mutants

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Histone H4 N-terminal tail mutants

Project description:A series of yeast carrying K->R mutations in the histone H4 N-terminal tail were profiled by gene expression array in mid-log phase. Keywords: repeat sample

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