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1.
J Phycol ; 57(2): 645-654, 2021 04.
Article in English | MEDLINE | ID: mdl-33314105

ABSTRACT

Foundation species provide physical structure that enhances the diversity and abundance of associated organisms. Canopy-forming seaweeds are known to act as foundation species on rocky shores by lowering temperature and desiccation stress. Direct solar radiation, including ultraviolet (UV) light, can also reduce photosynthetic rates in algae, cause oxidative stress and DNA damage. The reduction in UV exposure provided by an algal canopy could therefore be important for understory organisms, including the red alga Chondrus crispus on New England's (USA) rocky shores, and this relationship may be more important at higher tidal elevations with increased low-tide exposure time. In field experiments, we investigated the relationship between tidal elevation and an index of C. crispus UV exposure, the concentration of UV-absorbing pigments. Low on the shore, C. crispus grew without a canopy. Higher on the shore, in the mid-intertidal zone, C. crispus was found under the canopy-forming rockweed, Fucus distichus subsp. evanescens. At this elevation, C. crispus was shaded (>50%; >1 m above MLLW). We performed a canopy removal experiment that spanned the mid-zone where C. crispus and F. distichus subsp. evanescens co-occur and the low-zone (no canopy). Following canopy removal in the mid-zone, UV pigment concentrations increased with tidal elevation. After accounting for the effect of elevation, removal of the algal canopy resulted in UV-protective pigment concentrations 2-fold higher than in un-manipulated control plots. These results suggest that amelioration of solar UV exposure might be another mechanism by which canopy seaweeds, acting as foundation species, facilitate understory seaweeds on rocky shores.


Subject(s)
Chondrus , Fucus , Seaweed , Ecosystem , Plants
2.
BMC Evol Biol ; 20(1): 107, 2020 08 20.
Article in English | MEDLINE | ID: mdl-32819273

ABSTRACT

BACKGROUND: Amber has been reported from the Early Cretaceous Crato Formation, as isolated clasts or within plant tissues. Undescribed cones of uncertain gymnosperm affinity have also been recovered with amber preserved in situ. Here, we provide multiple lines of evidence to determine the botanical affinity of this enigmatic, conspicuous cone type, and to better understand the diversity of amber-source plants present in the Crato Formation and beyond. RESULTS: A new taxon of amber-bearing pollen cone Araripestrobus resinosus gen. nov. et sp. nov. is described here from complete cones and characteristic disarticulated portions. The best-preserved cone portion has both in situ amber infilling the resin canals inside the preserved microsporophyll tissues and pollen of the Eucommiidites-type. This places this genus within the Erdtmanithecales, an incompletely known gymnosperm group from the Mesozoic. FTIR analysis of the in situ amber indicates a potential araucariacean conifer affinity, although affinity with cupressacean conifers cannot be definitely ruled out. Pyr-GC-MS analysis of the Araripestrobus resinosus gen. nov. et sp. nov. in situ fossil resin shows that it is a mature class Ib amber, thought to indicate affinities with araucariacean and cupressacean, but not pinaceous, conifers. This is the first confirmed occurrence of this class of amber in the Crato Formation flora and in South America, except for an archaeological sample from Laguna Guatavita, Colombia. CONCLUSIONS: The combined results of the cones' novel gross morphology and the analyses of the in situ amber and pollen clearly indicate that the new taxon of resinous gymnosperm pollen cones from the Crato Formation is affiliated with Erdtmanithecales. The cone morphology is very distinct from all known pollen cone types of this extinct plant group. We therefore assume that the plant group that produced Eucommiidites-type pollen is much more diverse in habits than previously thought. Moreover, the diversity of potential amber source plants from the Crato Formation is now expanded beyond the Araucariaceae and the Cheirolepidiaceae to include this member of the Erdtmanithecales. Despite dispersed Eucommiidites pollen being noted from the Crato Formation, this is the first time macrofossils of Erdtmanithecales have been recognized from the Early Cretaceous of South America.


Subject(s)
Amber , Biodiversity , Cycadopsida/classification , Fossils , Brazil , Pollen
3.
Sci Rep ; 10(1): 3401, 2020 02 25.
Article in English | MEDLINE | ID: mdl-32099018

ABSTRACT

Some liquid plant exudates (e.g. resin) can be found preserved in the fossil record. However, due to their high solubility, gums have been assumed to dissolve before fossilisation. The visual appearance of gums (water-soluble polysaccharides) is so similar to other plant exudates, particularly resin, that chemical testing is essential to differentiate them. Remarkably, Welwitschiophyllum leaves from Early Cretaceous, Brazil provide the first chemical confirmation of a preserved gum. This is despite the leaves being exposed to water twice during formation and subsequent weathering of the Crato Formation. The Welwitschiophyllum plant shares the presence of gum ducts inside leaves with its presumed extant relative the gnetalean Welwitschia. This fossil gum presents a chemical signature remarkably similar to the gum in extant Welwitschia and is distinct from those of fossil resins. We show for the first time that a water-soluble plant exudate has been preserved in the fossil record, potentially allowing us to recognise further biomolecules thought to be lost during the fossilisation process.


Subject(s)
Fossils , Plant Gums/chemistry , Plant Leaves/chemistry , Brazil
4.
Int J Mol Med ; 16(2): 251-6, 2005 Aug.
Article in English | MEDLINE | ID: mdl-16012757

ABSTRACT

cAMP response element-binding protein (CREB)-binding protein (CBP) is a multifunctional transcriptional co-activator that plays important roles in cell proliferation and differentiation. CBP is expressed in murine embryonic orofacial tissue and is developmentally regulated. To identify nuclear factors associating with CBP in developing orofacial tissue, a yeast two-hybrid screen of a cDNA library derived from embryonic orofacial tissue from gestational days 11-13 mouse embryos was conducted. The carboxy terminal region of CBP (including the C/H3 region) was utilized as a bait. C53, a 57 kDa protein known to bind to the p25 activator of cyclin-dependent kinase 5, was identified as a novel binding partner of CBP. The association of C53 with CBP was confirmed in vitro by glutathione S-transferase pull-down assays, and in vivo by co-immunoprecipitation. Reporter assays demonstrated that C53 had little effect on CBP mediated transcriptional activation. These results identify C53 as a novel binding partner for CBP. Recent research on presenilin-loss induced neurodegeneration demonstrated decreased expression of CBP and increased levels of the Cdk5 activator p25, both C53 binding proteins, suggesting that C53 might play a role in regulating neuronal proliferation, migration and/or differentiation in embryonic development.


Subject(s)
Carrier Proteins/metabolism , Nerve Tissue Proteins/metabolism , Animals , Carrier Proteins/genetics , Cell Cycle Proteins , Cell Line , DNA, Complementary/genetics , DNA, Complementary/isolation & purification , Female , Gene Expression Regulation, Developmental , Glutathione Transferase/genetics , Glutathione Transferase/metabolism , Immunoprecipitation , Male , Mice , Mice, Inbred ICR , Mouth/embryology , Mouth/metabolism , Nerve Tissue Proteins/genetics , Plasmids/genetics , Pregnancy , Protein Binding , Proteins , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Saccharomyces cerevisiae/genetics , Tumor Suppressor Proteins , Two-Hybrid System Techniques
5.
J Interferon Cytokine Res ; 25(6): 321-7, 2005 Jun.
Article in English | MEDLINE | ID: mdl-15957955

ABSTRACT

cAMP response element binding protein (CREB)-binding protein (CBP) is a multifunctional transcriptional coactivator that plays important roles in gene regulation. CBP is expressed in murine embryonic orofacial tissue, where it is developmentally regulated. To identify nuclear factors associated with CBP in developing orofacial tissue, a yeast two-hybrid screen of a cDNA library derived from embryonic orofacial tissue from gestational days 11-13 mouse embryos was conducted. Using the carboxy terminal region of CBP as bait, the protein inhibitor of activated Stat1 (PIAS1) was identified as a novel CBP binding protein. The association of PIAS1 with CBP was confirmed in vitro by glutathione S-transferase (GST) pull-down assays and in vivo by coimmunoprecipitation. Reporter assays demonstrated that PIAS1 inhibited CBP-mediated transcriptional activation in the presence or absence of transforming growth factor-beta (TGF-beta). These results identify PIAS1 as a novel binding partner for CBP and inhibitor of CBP-mediated transcription, suggesting that PIAS1 might play a role in regulating cell proliferation, migration, and differentiation during embryonic development.


Subject(s)
Nuclear Proteins/metabolism , Proteins/metabolism , Trans-Activators/metabolism , Animals , CREB-Binding Protein , Female , Male , Mice , Mice, Inbred ICR , Nuclear Proteins/genetics , Protein Binding/genetics , Protein Binding/physiology , Protein Inhibitors of Activated STAT , Proteins/genetics , Trans-Activators/genetics , Transforming Growth Factor beta/metabolism , Two-Hybrid System Techniques
6.
Biochem Biophys Res Commun ; 329(3): 1010-7, 2005 Apr 15.
Article in English | MEDLINE | ID: mdl-15752756

ABSTRACT

cAMP response element-binding protein (CREB)-binding protein (CBP) plays an important role as a general co-integrator of multiple signaling pathways and interacts with a large number of transcription factors and co-factors, through its numerous protein-binding domains. To identify nuclear factors associated with CBP in developing orofacial tissue, a yeast two-hybrid screen of a cDNA library derived from orofacial tissue from gestational day 11 to 13 mouse embryos was conducted. Using the carboxy terminus (amino acid residues 1676-2441) of CBP as bait, several novel proteins that bind CBP were identified, including an Msx-interacting-zinc finger protein, CDC42 interaction protein 4/thyroid hormone receptor interactor 10, SH3-domain GRB2-like 1, CCR4-NOT transcription complex subunit 3, adaptor protein complex AP-1 beta1 subunit, eukaryotic translation initiation factor 2B subunit 1 (alpha), and cyclin G-associated kinase. Results of the yeast two-hybrid screen were confirmed by glutathione S-transferase pull-down assays. The identification of these proteins as novel CBP-binding partners allows exploration of new mechanisms by which CBP regulates and integrates diverse cell signaling pathways.


Subject(s)
Connective Tissue/embryology , Connective Tissue/metabolism , Cyclic AMP Response Element-Binding Protein/metabolism , Face/embryology , Maxillofacial Development/physiology , Protein Interaction Mapping , Transcription Factors/metabolism , Animals , Cells, Cultured , Mice , Mouth/embryology , Mouth/metabolism , Protein Binding
7.
Genesis ; 39(1): 58-64, 2004 May.
Article in English | MEDLINE | ID: mdl-15124228

ABSTRACT

This study is the first to report a unique genetic strategy to permanently label mammalian neural crest cells (NCC) with a fluorescent marker, selectively isolate the labeled NCC or their derivatives during murine ontogenesis by laser capture microdissection (LCM), and prepare molecular components, such as RNA, for selective gene expression analyses. Through utilization of a Cre recombinase/loxP system, a genetic strategy that has been used repeatedly to achieve tissue-specific activation of reporter transgenes in mice, a novel two-component mouse model was created in which neural crest cells (and their progeny) are indelibly marked throughout the pre- and postnatal lifespan of the organism. To generate this mouse model, a Wnt1-Cre transgenic line was crossed with a mouse line expressing a conditional reporter transgene ("floxed" enhanced green fluorescent protein). Resulting offspring, expressing both the Wnt1-Cre and "floxed" EGFP alleles, demonstrated EGFP expression in the NCC and all of their derivatives throughout embryonic, postnatal, and adult stages. In the present study, EGFP-labeled cranial NCC from the first branchial arch of gestational day 9.5 murine embryos were visualized in frozen tissue sections and isolated by LCM under epifluorescence optics. RNA was extracted from "captured" cells and amplified by double-stranded cDNA synthesis and in vitro transcription. Amplified mRNA samples from "captured" cells were evaluated by TaqMan quantitative, real-time PCR for the expression of a panel of NCC gene markers. The molecular genetic strategy delineated in this report will facilitate future embryo-genomic and -proteomic analyses of mammalian NCC that will serve to further our understanding of these pluripotent embryonic progenitor cells.


Subject(s)
Embryo, Mammalian/cytology , Embryo, Nonmammalian , Fluorescent Dyes/chemistry , Neural Crest/cytology , Base Sequence , DNA Primers , Lasers , Polymerase Chain Reaction
8.
Biochem Biophys Res Commun ; 312(4): 1185-90, 2003 Dec 26.
Article in English | MEDLINE | ID: mdl-14651998

ABSTRACT

The TGFbetas, a family of secreted polypeptide growth factors, are critical regulators of mammalian orofacial development. The importance of the TGFbetas in development of the orofacial region in mice is underscored by the resulting orofacial clefts in mice with targeted deletion of either TGFbeta2 or TGFbeta3 and most recently, a conditional knockout of the type II TGFbeta receptor (TbetaRII) gene. The TGFbetas signal via binding to specific cell surface receptors which, in turn, activates translocation of the nucleocytoplasmic Smad transcriptional regulators. Smads 2 and 3 are TGFbeta-specific transcriptional regulators that bind DNA through their conserved MH1 domains and activate or inhibit transcription of TGFbeta-responsive genes through their MH2 domains. To search for novel Smad binding proteins expressed in developing murine orofacial tissue, a yeast two-hybrid assay was utilized to screen a cDNA expression library constructed from fetal murine orofacial tissue. Several novel Smad binding proteins were identified. These include a putative zinc finger protein (ZNF198), peroxisomal biogenesis factor 6 (Pex6), eucaryotic translation initiation factor 4E nuclear import factor 1 (4-ET), and splicing factor 3b subunit 2 (SF3b2). Results of the yeast two-hybrid screen were verified by GST pull-down assays which confirmed the interaction of these proteins with the MH2 domain of Smad 3, and also indicated interaction of these proteins with additional Smad family members. The identification of these proteins as Smad binding partners allows exploration of new mechanisms whereby TGFbeta signaling may be regulated, and reveals additional potential interactions with other signaling pathways.


Subject(s)
DNA-Binding Proteins/metabolism , Face/embryology , Face/physiology , Mouth/embryology , Mouth/metabolism , Signal Transduction/physiology , Trans-Activators/metabolism , Transforming Growth Factor beta/metabolism , Animals , Carrier Proteins/metabolism , DNA-Binding Proteins/analysis , DNA-Binding Proteins/classification , Male , Smad Proteins , Smad3 Protein , Trans-Activators/analysis , Trans-Activators/classification , Transcription, Genetic/physiology , Two-Hybrid System Techniques
9.
FEBS Lett ; 539(1-3): 167-73, 2003 Mar 27.
Article in English | MEDLINE | ID: mdl-12650946

ABSTRACT

A yeast two-hybrid screen was utilized to identify novel Smad 3 binding proteins expressed in developing mouse orofacial tissue. Three proteins (Erbin, Par-3, and Dishevelled) were identified that share several similar structural and functional characteristics. Each contains at least one PDZ domain and all have been demonstrated to play a role in the establishment and maintenance of cell polarity. In GST (glutathione S-transferase) pull-down assays, Erbin, Par-3, and Dishevelled bound strongly to the isolated MH2 domain of Smad 3, with weaker binding to a full-length Smad 3 protein. Failure of Erbin, Par-3, and Dishevelled to bind to a Smad 3 mutant protein that was missing the MH2 domain confirms that the binding site resides within the MH2 domain. Erbin, Par-3, and Dishevelled also interacted with the MH2 domains of other Smads, suggesting broad Smad binding specificity. Dishevelled and Erbin mutant proteins, in which the PDZ domain was removed, still retained their ability to bind Smad 3, albeit with lower affinity. While transforming growth factor beta (TGFbeta) has been suggested to alter cell polarity through a Smad-independent mechanism involving activation of members of the RhoA family of GTP binding proteins, the observation that Smads can directly interact with proteins involved in cell polarity, as shown in the present report, suggests an additional means by which TGFbeta could alter cell polarity via a Smad-dependent signaling mechanism.


Subject(s)
Carrier Proteins/physiology , Cell Adhesion Molecules , DNA-Binding Proteins/metabolism , Phosphoproteins/physiology , Trans-Activators/metabolism , Adaptor Proteins, Signal Transducing , Animals , Carrier Proteins/metabolism , Cell Cycle Proteins , Cell Polarity , Dishevelled Proteins , Female , Intracellular Signaling Peptides and Proteins , Male , Mice , Mice, Inbred ICR , Phosphoproteins/metabolism , Smad3 Protein , Two-Hybrid System Techniques
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