Functional and Structural Roles of Coiled Coils

Hartmann, M.D.

doi:10.1007/978-3-319-49674-0_3

Cited by 31 publications

(23 citation statements)

References 143 publications

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“…On an entirely different note, the present work also leads to a deeper understanding of the fundamental principles underlying the evolution, stability and dynamics of a coiled coil in a physiological context. Coiled coils are among the most intensively studied protein folds ( Hartmann, 2017 ), can be characterized and described from first principles ( Crick, 1953 ; Lupas et al, 2017 ) and have become a preferred target for protein design ( Woolfson, 2017 ). The present L1 retrotransposition assay could therefore serve as one of the most sensitive assay systems for testing coiled coil designs in a cellular environment.…”

Section: Discussionmentioning

confidence: 99%

Human LINE-1 retrotransposition requires a metastable coiled coil and a positively charged N-terminus in L1ORF1p

Khazina

Weichenrieder

2018

eLife

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LINE-1 (L1) is an autonomous retrotransposon, which acted throughout mammalian evolution and keeps contributing to human genotypic diversity, genetic disease and cancer. L1 encodes two essential proteins: L1ORF1p, a unique RNA-binding protein, and L1ORF2p, an endonuclease and reverse transcriptase. L1ORF1p contains an essential, but rapidly evolving N-terminal portion, homo-trimerizes via a coiled coil and packages L1RNA into large assemblies. Here, we determined crystal structures of the entire coiled coil domain of human L1ORF1p. We show that retrotransposition requires a non-ideal and metastable coiled coil structure, and a strongly basic L1ORF1p amino terminus. Human L1ORF1p therefore emerges as a highly calibrated molecular machine, sensitive to mutation but functional in different hosts. Our analysis rationalizes the locally rapid L1ORF1p sequence evolution and reveals striking mechanistic parallels to coiled coil-containing membrane fusion proteins. It also suggests how trimeric L1ORF1p could form larger meshworks and indicates critical novel steps in L1 retrotransposition.

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Section: Discussionmentioning

confidence: 99%

Human LINE-1 retrotransposition requires a metastable coiled coil and a positively charged N-terminus in L1ORF1p

Khazina

Weichenrieder

2018

eLife

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“…As summarized in excellent articles on the topic, coiled coils are architecturally well‐understood to the extent that their structures can be predicted with high levels of confidence . Given the preeminence of coiled coils in SHK signaling, a brief discussion in the present context is nonetheless warranted; for an authoritative, detailed treatise, the reader is referred to pertinent reviews . In coiled coils, two or more α‐helices are in register and are wound around a common central (or, superhelical) axis, either in parallel or antiparallel orientation.…”

Section: Signal Transmission Through α‐Helical Bundles and Linkersmentioning

confidence: 99%

“…Often, the linker helix is also referred to as the signaling or S helix. 131 As summarized in excellent articles on the topic, coiled coils are architecturally wellunderstood [132][133][134] to the extent that their structures can be predicted with high levels of confidence. 135 Given the preeminence of coiled coils in SHK signaling, a brief discussion in the present context is nonetheless warranted; for an authoritative, detailed treatise, the reader is referred to pertinent reviews.…”

Section: The Structure Of α-Helical Coiled Coilsmentioning

confidence: 99%

“…135 Given the preeminence of coiled coils in SHK signaling, a brief discussion in the present context is nonetheless warranted; for an authoritative, detailed treatise, the reader is referred to pertinent reviews. [132][133][134] In coiled coils, two or more α-helices are in register and are wound around a common central (or, superhelical) axis, either in parallel or antiparallel orientation. The resultant helical assembly is stabilized by knobsinto-holes packing where sidechains of one helix (i.e., the "knobs") periodically protrude into depressions (i.e., the "holes") formed by sidechains of the partner helix or helices, respectively ( Figure 6A).…”

Section: The Structure Of α-Helical Coiled Coilsmentioning

confidence: 99%

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Signal transduction in photoreceptor histidine kinases

Möglich

2019

Protein Science

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Two‐component systems (TCS) constitute the predominant means by which prokaryotes read out and adapt to their environment. Canonical TCSs comprise a sensor histidine kinase (SHK), usually a transmembrane receptor, and a response regulator (RR). In signal‐dependent manner, the SHK autophosphorylates and in turn transfers the phosphoryl group to the RR which then elicits downstream responses, often in form of altered gene expression. SHKs also catalyze the hydrolysis of the phospho‐RR, hence, tightly adjusting the overall degree of RR phosphorylation. Photoreceptor histidine kinases are a subset of mostly soluble, cytosolic SHKs that sense light in the near‐ultraviolet to near‐infrared spectral range. Owing to their experimental tractability, photoreceptor histidine kinases serve as paradigms and provide unusually detailed molecular insight into signal detection, decoding, and regulation of SHK activity. The synthesis of recent results on receptors with light‐oxygen‐voltage, bacteriophytochrome and microbial rhodopsin sensor units identifies recurring, joint signaling strategies. Light signals are initially absorbed by the sensor module and converted into subtle rearrangements of α helices, mostly through pivoting and rotation. These conformational transitions propagate through parallel coiled‐coil linkers to the effector unit as changes in left‐handed superhelical winding. Within the effector, subtle conformations are triggered that modulate the solvent accessibility of residues engaged in the kinase and phosphatase activities. Taken together, a consistent view of the entire trajectory from signal detection to regulation of output emerges. The underlying allosteric mechanisms could widely apply to TCS signaling in general.

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“…Coiled coils are ubiquitous structural units of proteins . They may occur alone or as domains within larger proteins and fulfill many different functions (Hartmann, 2017;Truebestein and Leonard, 2016). Coiled coils are, for instance, essential components of the cellular skeleton and of motor proteins that contribute to cellular motility (Squire et al, 2017).…”

Section: Introductionmentioning

confidence: 99%