Genome evolution and the evolution of exon-shuffling — a review

Patthy, László

doi:10.1016/s0378-1119(99)00228-0

Cited by 392 publications

(281 citation statements)

References 87 publications

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“…The fact that intron/exon boundaries do not overlap with domain boundaries is also observed for other ancient multidomain proteins unique to metazoans. This probably results from a continual insertion and removal of introns (Patthy, 1999). This notion of ancientness is further supported by the lack of sequence identity among the eight MG domains, which do not show a single conserved amino-acid residue.…”

Section: Domain Organizationmentioning

confidence: 95%

Structural insights into the central complement component C3

Janssen

Gros

2007

Molecular Immunology

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C3 is a central protein of the complement system, which is important to immune defense and provides a link between innate and adaptive immunity. Three pathways of complement activation converge at the activation of C3 yielding a diverse set of biological responses. This versatile and flexible molecule interacts with various proteins to fulfill its functions. Here we review recent insights gained from the crystal structure determinations of human, native C3 and its physiological down-regulation product C3c. The data provided, for the first time, a complete and detailed view of the composition and arrangement of the domains in C3. Comparison of C3 with C3c indicates marked flexibility of the molecule, particularly in the ␣-chain. We discuss the observed domain rearrangements, conformational changes and the location of various protein binding sites. These detailed, and structural, insights are important for developing models of the molecular mechanisms underlying the diverse biological activities of this large and complex molecule.

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Section: Domain Organizationmentioning

confidence: 95%

Structural insights into the central complement component C3

Janssen

Gros

2007

Molecular Immunology

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“…Experimental evidence indicates that a non-random tendency exists for introns to be located in interdomain regions of proteins (Patthy, 1999;Liu and Altman, 2003) and that introns have a propensity to avoid secondary structure elements such as alpha-helices and beta-strands (Contreras- Moreira et al, 2003). Therefore, we investigated the possible correlation between intron gain/loss events and the secondary structure of Neuroligin proteins.…”

Section: Correlation Of Intron Gain/ Loss Events and Secondary Proteimentioning

confidence: 99%

Characterization of the neuroligin gene family expression and evolution in zebrafish

Rissone¹,

Sangiorgio²,

Monopoli³

et al. 2010

Developmental Dynamics

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Neuroligins constitute a family of transmembrane proteins localized at the postsynaptic side of both excitatory and inhibitory synapses of the central nervous system. They are involved in synaptic function and maturation and recent studies have linked mutations in specific human Neuroligins to mental retardation and autism. We isolated the human Neuroligin homologs in Danio rerio. Next, we studied their gene structures and we reconstructed the evolution of the Neuroligin genes across vertebrate phyla. Using reverse-transcriptase polymerase chain reaction, we analyzed the expression and alternative splicing pattern of each gene during zebrafish embryonic development and in different adult organs. By in situ hybridization, we analyzed the temporal and spatial expression pattern during embryonic development and larval stages and we found that zebrafish Neuroligins are expressed throughout the nervous system. Globally, our results indicate that, during evolution, specific subfunctionalization events occurred within paralogous members of this gene family in zebrafish. Developmental Dynamics 239:688-702,

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“…Conventional comparative analyses of genes with diverged functions and the creation of new genes in the laboratory have contributed greatly to our understanding of evolutionary forces and functional divergence (2,3). Building on these approaches, an examination of recently evolved genes provides a window through which both the origin and subsequent divergence are directly observable.…”

mentioning

confidence: 99%

Evolving protein functional diversity in new genes of Drosophila

Zhang

Dean

Brunet

et al. 2004

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

107

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The mechanism by which protein functional diversity expands is an important evolutionary issue. Studies of recently evolved chimeric genes permit direct investigation of the origin of new protein functions before they become obscured by subsequent evolution. Found in several African Drosophila species, jingwei (jgw), a recently evolved gene with a domain derived from the still extant short-chain alcohol dehydrogenase (ADH) through retroposition, provides an opportunity to examine this previously undescribed process directly. We expressed JGW proteins in a microbial expression system and, after purification, investigated their enzymatic properties. We found that, unexpectedly, positive Darwinian selection for amino acid replacements outside the active site of JGW produced a novel dehydrogenase with altered substrate specificity compared with the ancestral ADH. Instead of detoxifying and assimilating ethanol like its Adh parental gene, we observe that JGW efficiently utilizes long-chain primary alcohols found in hormone and pheromone metabolism. These data suggest that protein functional diversity can expand rapidly under the joint forces of exon shuffling, gene duplication, and natural selection.

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Genome evolution and the evolution of exon-shuffling — a review

Cited by 392 publications

References 87 publications

Structural insights into the central complement component C3

Structural insights into the central complement component C3

Characterization of the neuroligin gene family expression and evolution in zebrafish

Evolving protein functional diversity in new genes of Drosophila

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