Topological characteristics of helical repeat protein

Groves, Matthew R.; Barford, David

doi:10.1016/s0959-440x(99)80052-9

Cited by 318 publications

(283 citation statements)

References 31 publications

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“…However, armadillo repeats are just one among several different types of repeats which are able to generate long alpha-helical structures known as ''Armadillo-like helical domains'' (InterPro domain no. IPR011989 [Groves and Barford 1999]). Most significantly, InterProScan detected these domains in 8 of the 10 sequences shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

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Ancient Origin of the Parkinson Disease Gene LRRK2

Marı́n

2008

J Mol Evol

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Dominant mutations in the LRRK2 gene, a member of the Roco family, cause both familial and sporadic Parkinson disease. LRRK genes had so far been detected only in bilaterian animals. In deuterostomes, including humans, two LRRK genes (LRRK1 and LRRK2) exist, while in protostomes a single LRRK gene has been found. In this study, I combine structural and phylogenetic analyses to show that the cnidarian Nematostella vectensis has four LRRK genes. One of them is a bona fide orthologue of the human LRRK2 gene, demonstrating that this gene has an ancient origin. Two others are, respectively, orthologues of the deuterostome LRRK1 and the protostome LRRK genes. The fourth gene is probably cnidarian-specific. This precise characterization of the early evolution of LRRK genes in animals has important implications, because it indicates that the Drosophila and Caenorhabditis LRRK genes, which are studied to gain an understanding of LRRK2 function, are not true orthologues of the human Parkinson disease gene. Novel functional insights are also gained by comparison of the structures of LRRK2 genes in distantly related species.

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Section: Resultsmentioning

confidence: 99%

“…Thus, we may conclude that LRRK2 proteins contain a peculiar Armadillo-like helical domain, absent from the rest of LRRK proteins. This kind of structure is considered to be a protein-protein interaction surface (Groves and Barford 1999).…”

Section: Resultsmentioning

confidence: 99%

Ancient Origin of the Parkinson Disease Gene LRRK2

Marı́n

2008

J Mol Evol

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“…Tandem repeats of distinct helical repeats like TPR, PPR, ARM (armadillo) and HEAT that combine to create extended superhelical structures are thought to represent primitive structures which have been duplicated and evolved for diverse and specialized protein-protein recognition interfaces among diverse cellular compartments [6,7]. The most extensively studied example of the ARM repeat is the functionally pleiotropic β-catenin that includes membrane to nucleus signaling while interacting with a series of partners along the way [7]. The PPR repeat, distinct from the TPR repeat, constitutes over 200 Arabidopsis gene products, two thirds of which are targeted to mitochondria and chloroplasts [6].…”

Section: Definition Of the Lrp Tandem Repeatmentioning

confidence: 99%

“…BSF binds to the 3'-untranslated region of bicoid mRNA and contributes to its stabilization [8]. HEAT motifs in particular have been refined for roles in specialized nuclear targeting apparatuses that respond to extranuclear events [7] and in chromosome dynamics during mitosis [9].…”

Section: Definition Of the Lrp Tandem Repeatmentioning

confidence: 99%

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Sequence Analysis of LRPPRC and Its SEC1 Domain Interaction Partners Suggests Roles in Cytoskeletal Organization, Vesicular Trafficking, Nucleocytosolic Shuttling, and Chromosome Activity

2002

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LRPPRC (originally called LRP130) is an intracellular 130-kDa leucine-rich protein that copurifies with the FGF receptor from liver cell extracts and has been detected in diverse multiprotein complexes from the cell membrane, cytoskeleton and nucleus. Here we report results of a sequence homology analysis of LRPPRC and its SEC1 domain interactive partners. Twenty-three copies of tandem repeats that are similar to PPR, TPR and HEAT repeats characterize the LRPPRC sequence. The N-terminus exhibits multiple copies of leucine-rich nuclear transport signals followed by ENTH, DUF28 and SEC1 homology domains. We used the SEC1 domain to trap interactive partners expressed from a human liver cDNA library. Interactive C19ORF5 (XP_038600) exhibited a strong homology to microtubule-associated proteins (MAP) and a potential arginine-rich mRNA binding motif. UXT (XP_033860) exhibited α-helical properties homologous to the actin-associated spectrin repeat and L/I heptad repeats in mobile transcription factors. C6ORF34 (XP_004305) was homologous to the non-DNA binding C-terminus of the E. coli Rob transcription factor. CECR2 (AAK15343) exhibited a transcription factor AT-hook motif next to two bromodomains and a homology to guanylate-binding protein 1. Taken together these features suggest a regulatory role of LRPPRC and its SEC1 domain-interactive partners in integration of cytoskeletal networks with vesicular trafficking, nucleocytosolic shuttling, chromosome remodeling and transcription.

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The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

1999

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The tetratricopeptide repeat (TPR) motif is a protein‐protein interaction module found in multiple copies in a number of functionally different proteins that facilitates specific interactions with a partner protein(s). Three‐dimensional structural data have shown that a TPR motif contains two antiparallel α‐helices such that tandem arrays of TPR motifs generate a right‐handed helical structure with an amphipathic channel that might accommodate the complementary region of a target protein. Most TPR‐containing proteins are associated with multiprotein complexes, and there is extensive evidence indicating that TPR motifs are important to the functioning of chaperone, cell‐cycle, transcription, and protein transport complexes. The TPR motif may represent an ancient protein‐protein interaction module that has been recruited by different proteins and adapted for specific functions. BioEssays 1999;21:932–939. © 1999 John Wiley & Sons, Inc.

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Topological characteristics of helical repeat protein

Cited by 318 publications

References 31 publications

Ancient Origin of the Parkinson Disease Gene LRRK2

Ancient Origin of the Parkinson Disease Gene LRRK2

Sequence Analysis of LRPPRC and Its SEC1 Domain Interaction Partners Suggests Roles in Cytoskeletal Organization, Vesicular Trafficking, Nucleocytosolic Shuttling, and Chromosome Activity

The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

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