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  1. Article ; Online: Positive Selection in Rapidly Evolving Plastid-Nuclear Enzyme Complexes.

    Rockenbach, Kate / Havird, Justin C / Monroe, J Grey / Triant, Deborah A / Taylor, Douglas R / Sloan, Daniel B

    Genetics

    2016  Volume 204, Issue 4, Page(s) 1507–1522

    Abstract: Rates of sequence evolution in plastid genomes are generally low, but numerous angiosperm lineages exhibit accelerated evolutionary rates in similar subsets of plastid genes. These genes include clpP1 and accD, which encode components of the caseinolytic ...

    Abstract Rates of sequence evolution in plastid genomes are generally low, but numerous angiosperm lineages exhibit accelerated evolutionary rates in similar subsets of plastid genes. These genes include clpP1 and accD, which encode components of the caseinolytic protease (CLP) and acetyl-coA carboxylase (ACCase) complexes, respectively. Whether these extreme and repeated accelerations in rates of plastid genome evolution result from adaptive change in proteins (i.e., positive selection) or simply a loss of functional constraint (i.e., relaxed purifying selection) is a source of ongoing controversy. To address this, we have taken advantage of the multiple independent accelerations that have occurred within the genus Silene (Caryophyllaceae) by examining phylogenetic and population genetic variation in the nuclear genes that encode subunits of the CLP and ACCase complexes. We found that, in species with accelerated plastid genome evolution, the nuclear-encoded subunits in the CLP and ACCase complexes are also evolving rapidly, especially those involved in direct physical interactions with plastid-encoded proteins. A massive excess of nonsynonymous substitutions between species relative to levels of intraspecific polymorphism indicated a history of strong positive selection (particularly in CLP genes). Interestingly, however, some species are likely undergoing loss of the native (heteromeric) plastid ACCase and putative functional replacement by a duplicated cytosolic (homomeric) ACCase. Overall, the patterns of molecular evolution in these plastid-nuclear complexes are unusual for anciently conserved enzymes. They instead resemble cases of antagonistic coevolution between pathogens and host immune genes. We discuss a possible role of plastid-nuclear conflict as a novel cause of accelerated evolution.
    MeSH term(s) Acetyl-CoA Carboxylase/genetics ; Chloroplast Proteins/genetics ; Endopeptidase Clp/genetics ; Evolution, Molecular ; Phylogeny ; Plant Proteins/genetics ; Polymorphism, Genetic ; Selection, Genetic ; Silene/classification ; Silene/genetics ; Silene/metabolism
    Chemical Substances Chloroplast Proteins ; Plant Proteins ; Endopeptidase Clp (EC 3.4.21.92) ; Acetyl-CoA Carboxylase (EC 6.4.1.2)
    Language English
    Publishing date 2016-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2167-2
    ISSN 1943-2631 ; 0016-6731
    ISSN (online) 1943-2631
    ISSN 0016-6731
    DOI 10.1534/genetics.116.188268
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Cross-talk between diverse serine integrases.

    Singh, Shweta / Rockenbach, Kate / Dedrick, Rebekah M / VanDemark, Andrew P / Hatfull, Graham F

    Journal of molecular biology

    2013  Volume 426, Issue 2, Page(s) 318–331

    Abstract: Phage-encoded serine integrases are large serine recombinases that mediate integrative and excisive site-specific recombination of temperate phage genomes. They are well suited for use in heterologous systems and for synthetic genetic circuits as the ... ...

    Abstract Phage-encoded serine integrases are large serine recombinases that mediate integrative and excisive site-specific recombination of temperate phage genomes. They are well suited for use in heterologous systems and for synthetic genetic circuits as the attP and attB attachment sites are small (<50 bp), there are no host factor or DNA supercoiling requirements, and they are strongly directional, doing only excisive recombination in the presence of a recombination directionality factor. Combining different recombinases that function independently and without cross-talk to construct complex synthetic circuits is desirable, and several different serine integrases are available. However, we show here that these functions are not reliably predictable, and we describe a pair of serine integrases encoded by mycobacteriophages Bxz2 and Peaches with unusual and unpredictable specificities. The integrases share only 59% amino acid sequence identity and the attP sites have fewer than 50% shared bases, but they use the same attB site and there is non-reciprocal cross-talk between the two systems. The DNA binding specificities do not result from differences in specific DNA contacts but from the constraints imposed by the configuration of the component half-sites within each of the attachment site DNAs.
    MeSH term(s) Attachment Sites, Microbiological ; Base Sequence ; DNA, Bacterial/metabolism ; DNA, Viral/metabolism ; Electrophoretic Mobility Shift Assay ; Integrases/genetics ; Integrases/metabolism ; Molecular Sequence Data ; Mycobacteriophages/enzymology ; Prophages/enzymology ; Protein Binding ; Recombination, Genetic ; Sequence Homology, Amino Acid ; Serine/metabolism ; Substrate Specificity ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances DNA, Bacterial ; DNA, Viral ; Viral Proteins ; Serine (452VLY9402) ; Integrases (EC 2.7.7.-)
    Language English
    Publishing date 2013-10-22
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2013.10.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Cluster J mycobacteriophages: intron splicing in capsid and tail genes.

    Pope, Welkin H / Jacobs-Sera, Deborah / Best, Aaron A / Broussard, Gregory W / Connerly, Pamela L / Dedrick, Rebekah M / Kremer, Timothy A / Offner, Susan / Ogiefo, Amenawon H / Pizzorno, Marie C / Rockenbach, Kate / Russell, Daniel A / Stowe, Emily L / Stukey, Joseph / Thibault, Sarah A / Conway, James F / Hendrix, Roger W / Hatfull, Graham F

    PloS one

    2013  Volume 8, Issue 7, Page(s) e69273

    Abstract: Bacteriophages isolated on Mycobacterium smegmatis mc(2)155 represent many distinct genomes sharing little or no DNA sequence similarity. The genomes are architecturally mosaic and are replete with genes of unknown function. A new group of genomes ... ...

    Abstract Bacteriophages isolated on Mycobacterium smegmatis mc(2)155 represent many distinct genomes sharing little or no DNA sequence similarity. The genomes are architecturally mosaic and are replete with genes of unknown function. A new group of genomes sharing substantial nucleotide sequences constitute Cluster J. The six mycobacteriophages forming Cluster J are morphologically members of the Siphoviridae, but have unusually long genomes ranging from 106.3 to 117 kbp. Reconstruction of the capsid by cryo-electron microscopy of mycobacteriophage BAKA reveals an icosahedral structure with a triangulation number of 13. All six phages are temperate and homoimmune, and prophage establishment involves integration into a tRNA-Leu gene not previously identified as a mycobacterial attB site for phage integration. The Cluster J genomes provide two examples of intron splicing within the virion structural genes, one in a major capsid subunit gene, and one in a tail gene. These genomes also contain numerous free-standing HNH homing endonuclease, and comparative analysis reveals how these could contribute to genome mosaicism. The unusual Cluster J genomes provide new insights into phage genome architecture, gene function, capsid structure, gene mobility, intron splicing, and evolution.
    MeSH term(s) Amino Acid Sequence ; Bacteriolysis/genetics ; Base Composition ; Base Sequence ; Capsid Proteins/chemistry ; Capsid Proteins/genetics ; Cluster Analysis ; DNA Transposable Elements ; Gene Order ; Genome Size ; Genome, Viral ; Introns ; Molecular Sequence Data ; Mycobacteriophages/classification ; Mycobacteriophages/genetics ; Mycobacteriophages/ultrastructure ; Open Reading Frames ; Phylogeny ; RNA Splicing ; Viral Tail Proteins/chemistry ; Viral Tail Proteins/genetics ; Virion/ultrastructure ; Virus Integration/genetics
    Chemical Substances Capsid Proteins ; DNA Transposable Elements ; Viral Tail Proteins
    Language English
    Publishing date 2013-07-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0069273
    Database MEDical Literature Analysis and Retrieval System OnLINE

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