Backbone dynamics of dynein light chains

Wu, Hongwei; King, Stephen M.

doi:10.1002/cm.10108

Cited by 9 publications

(3 citation statements)

References 25 publications

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“…A number of proteins are now known to bind nonplant LC8 proteins, and in general two amino acid motifs allow LC8 binding: (K/R)XTQT and GIQVDR (for review, see Wu and King, 2003). We identified four amino acids in Hopie Gag responsible for the interaction with ZmLC8 and suggest G(I/V)XCXL as a possible LC8 interaction motif in plants.…”

Section: Sequences Critical For Gag/lc8 Interactionmentioning

confidence: 92%

The Sireviruses, a Plant-Specific Lineage of the Ty1/copia Retrotransposons, Interact with a Family of Proteins Related to Dynein Light Chain 8

2005

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Plant genomes are rich in long terminal repeat retrotransposons, and here we describe a plant-specific lineage of Ty1/copia elements called the Sireviruses. The Sireviruses vary greatly in their genomic organization, and many have acquired additional coding information in the form of an envelope-like open reading frame and an extended gag gene. Two-hybrid screens were conducted with the novel domain of Gag (the Gag extension) encoded by a representative Sirevirus from maize (Zea mays) called Hopie. The Hopie Gag extension interacts with a protein related to dynein light chain 8 (LC8). LC8 also interacts with the Gag extension from a Hopie homolog from rice (Oryza sativa). Amino acid motifs were identified in both Hopie Gag and LC8 that are responsible for the interaction. Two amino acids critical for Gag recognition map within the predicted LC8-binding cleft. Two-hybrid screens were also conducted with the Gag extension encoded by the soybean (Glycine max) SIRE1 element, and an interaction was found with light chain 6 (LC6), a member of the LC8 protein family. LC8 and LC6 proteins are components of the dynein microtubule motor, with LC8 being a versatile adapter that can bind many unrelated cellular proteins and viruses. Plant LC8 and LC6 genes are abundant and divergent, yet flowering plants do not encode other components of the dynein motor. Although, to our knowledge, no cellular roles for plant LC8 family members have been proposed, we hypothesize that binding of LC8 proteins to Gag aids in the movement of retrotransposon virus-like particles within the plant cell or possibly induces important conformational changes in the Gag protein.

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Section: Sequences Critical For Gag/lc8 Interactionmentioning

confidence: 92%

The Sireviruses, a Plant-Specific Lineage of the Ty1/copia Retrotransposons, Interact with a Family of Proteins Related to Dynein Light Chain 8

2005

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“…Both monomers contribute to the formation of two symmetrical grooves in the dimer that are the binding sites for two DYNC1I polypeptides reviewed in [161]. Adding DYNLL to an N-terminal polypeptide of DYNC1I in vitro increases the structural order of DYNC1I, suggesting that DYNLL is important for the assembly of a functional dynein complex [84].…”

Section: Cytoplasmic Dynein Light Chain Lc8 Gene Family (Dynll1 Dynlmentioning

confidence: 99%

Genetic Analysis of the Cytoplasmic Dynein Subunit Families

Pfister¹,

Shah²,

Hummerich³

et al. 2006

PLoS Genet

287

316

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Cytoplasmic dyneins, the principal microtubule minus-end-directed motor proteins of the cell, are involved in many essential cellular processes. The major form of this enzyme is a complex of at least six protein subunits, and in mammals all but one of the subunits are encoded by at least two genes. Here we review current knowledge concerning the subunits, their interactions, and their functional roles as derived from biochemical and genetic analyses. We also carried out extensive database searches to look for new genes and to clarify anomalies in the databases. Our analysis documents evolutionary relationships among the dynein subunits of mammals and other model organisms, and sheds new light on the role of this diverse group of proteins, highlighting the existence of two cytoplasmic dynein complexes with distinct cellular roles.

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“…This LC consists of an N-terminal helix followed by six ␤␤␣ motifs derived from the LRRs and a C-terminal helical domain that protrudes from the main protein axis defined by the LRR barrel (16). The orientation of the C-terminal helical region is controlled by two residues (Met 182 and Asp 185 ) that exhibit high backbone dynamics; the remainder of the protein is relatively rigid with the exception of both termini and a flexible leucine spine within one interaction surface (17,18). The C-terminal region is also highly charged: in mammals, the ␣9 helix is very acidic, whereas in Chlamydomonas and Trypanosoma, there are two conserved basic residues (Arg 189 and Arg 196 in Chlamydomonas) in addition to several Asp/Glu residues.…”

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confidence: 99%

Functional Architecture of the Outer Arm Dynein Conformational Switch

King

Patel‐King

2012

Journal of Biological Chemistry

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Background: Ciliary dyneins monitor and respond to the mechanical state or curvature of the microtubular axoneme. Results: NMR chemical shift mapping and binding assays define functional subdomains within a key component (LC1) of this system. Conclusion: LC1 provides a direct tether between a dynein motor unit and the microtubule that modulates motor function. Significance: This study provides insight into the mechanism by which dyneins are coordinated during ciliary beating.

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Backbone dynamics of dynein light chains

Cited by 9 publications

References 25 publications

The Sireviruses, a Plant-Specific Lineage of the Ty1/copia Retrotransposons, Interact with a Family of Proteins Related to Dynein Light Chain 8

The Sireviruses, a Plant-Specific Lineage of the Ty1/copia Retrotransposons, Interact with a Family of Proteins Related to Dynein Light Chain 8

Genetic Analysis of the Cytoplasmic Dynein Subunit Families

Functional Architecture of the Outer Arm Dynein Conformational Switch

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