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Evolution of collagen IV genes from a 54-base pair exon: A role for introns in gene evolution 总被引:1,自引:0,他引:1
Giovanna Butticè Paul Kaytes Jeanine D'Armiento Gabriel Vogeli Markku Kurkinen 《Journal of molecular evolution》1990,30(6):479-488
The exon structure of the collagen IV gene provides a striking example for collagen evolution and the role of introns in gene evolution. Collagen IV, a major component of basement membranes, differs from the fibrillar collagens in that it contains numerous interruptions in the triple helical Gly-X-Y repeat domain. We have characterized all 47 exons in the mouse alpha 2(IV) collagen gene and find two 36-, two 45-, and one 54-bp exons as well as one 99- and three 108-bp exons encoding the Gly-X-Y repeat sequence. All these exons sizes are also found in the fibrillar collagen genes. Strikingly, of the 24 interruption sequences present in the alpha 2-chain of mouse collagen IV, 11 are encoded at the exon/intron borders of the gene, part of one interruption sequence is encoded by an exon of its own, and the remaining interruptions are encoded within the body of exons. In such "fusion exons" the Gly-X-Y encoding domain is also derived from 36-, 45-, or 54-bp sequence elements. These data support the idea that collagen IV genes evolved from a primordial 54-bp coding unit. We furthermore interpret these data to suggest that the interruption sequences in collagen IV may have evolved from introns, presumably by inactivation of splice site signals, following which intronic sequences could have been recruited into exons. We speculated that this mechanism could provide a role for introns in gene evolution in general. 相似文献
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K C Minghetti V C Goswitz N E Gabriel J J Hill C A Barassi C D Georgiou S I Chan R B Gennis 《Biochemistry》1992,31(30):6917-6924
The cytochrome o complex is a bo-type ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli. This complex has a close structural and functional relationship with the eukaryotic and prokaryotic aa3-type cytochrome c oxidases. The specific activity, subunit composition, and metal content of the purified cytochrome o complex are not consistent for different preparative protocols reported in the literature. This paper presents a relatively simple preparation of the enzyme starting with a strain of Escherichia coli which overproduces the oxidase. The pure enzyme contains four subunits by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Partial amino acid sequence data confirm the identities of subunit I, II, and III from the SDS-PAGE analysis as the cyoB, cyoA, and cyoC gene products, respectively. A slight modification of the purification protocol yields an oxidase preparation that contains a possible fifth subunit which may be the cyoE gene product. The pure four-subunit enzyme contains 2 equivs of iron but only 1 equiv of copper. There is no electron paramagnetic resonance detectable copper in the purified enzyme. Hence, the equivalent of CuA of the aa3-type cytochrome c oxidases is absent in this quinol oxidase. There is also no zinc in the purified quinol oxidase. Finally, monoclonal antibodies are reported that interact with subunit II. One of these monoclonals inhibits the quinol oxidase activity of the detergent-solubilized, purified oxidase. Hence, although subunit II does not contain CuA and does not interact with cytochrome c, it still must have an important function in the bo-type ubiquinol oxidase. 相似文献
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2,4-dichlorophenoxyacetic (2,4-D) applied to excised leaves of Cassia fasciculata modified the dark-induced (scotonasty) and light-induced (photonasty) leaflet movements, showing that this compound acts on rapid turgor variation and the concomitant ion migrations, in particular K+. 2,4-D inhibited the scotonastic closure in a dose-dependent manner from 10–8
M to 10–5
M and promoted the photonastic opening in the same range of concentrations. The compound acted rapidly since a treatment as short as 5 min gave an obvious effect on the motile reaction; however, a lag period of 45–60 min was needed to observe its effect. Although 2,4-D is a weak acid, its greatest physiological efficiency was obtained with pH values close to neutrality. The physiological results are discussed in relation to the chemical properties and the characteristics of transport of the molecule.Abbreviations ABA
abscisic acid
- 6-BAP
6-benzylaminopurine
- 2,4-D
2,4 dichlorophenoxyacetic acid
- GA3
gibberellic acid
- HEPES
N-[2-hydroxyethyl] piperazine-N-[2-ethanesulphonic acid]
- IAA
indole-3-acetic acid
- NAA
1-naphthaleneacetic acid
- MES
2-(N-morpholino)-ethanesulphonic acid 相似文献
47.
Akira Akabayashi C.T.B.V. Zaia James I. Koenig Steven M. Gabriel Ivan Silva Sarah F. Leibowitz 《Peptides》1994,15(8):1437-1444
The peptide galanin (GAL), when injected into the rat hypothalamus, is known to stimulate feeding behavior and affect the secretion of various hormones, including insulin and the adrenal steroid, corticosterone. To determine whether endogenous peptide levels shift in relation to natural rhythms of feeding and circulating hormone levels, rats were sacrificed at different times of the light/dark cycle, and their GAL levels were measured, via radioimmunoassay, in medial hypothalamic dissections and micropunched hypothalamic areas. The results suggest the existence of two distinct diurnal rhythms for hypothalamic GAL. One rhythm, detected exclusively in the area of the SCN, is characterized by bimodal peaks of GAL, threefold higher than basal peptide levels, around the onset of the dark and light periods. The second rhythm shows a single peak of GAL towards the middle of the nocturnal feeding cycle, specifically between the third and sixth hour. This latter rhythm is evident in the dorsal region of the medial hypothalamus, localized specifically to the lateral portion of the PVN. Moreover, it is inversely related to circulating insulin but unrelated to the adrenal steroids, suggesting a possible association between this pancreatic hormone and GAL in the PVN. 相似文献
48.
Gabriel Gutiérrez Josep Casadesús Jose L. Oliver Antonio Marine 《Journal of molecular evolution》1994,39(4):340-346
E. coli genes that contain a high frequency of the tetranucleotide CTAG are also rich in the tetramers CTTG, CCTA, CCAA, TTGG, TAGG, and CAAG (group-I tetramers). Conversely, E. coli genes lacking CTAG are rich in the tetranucleotides CCTG, CCAG, CTGG, and CAGG (group-II tetramers). These two gene samples differ also in codon usage, amino acid composition, frequency of Dcm sites, and contrast vocabularies. Group-I tetramers have in common that they are depleted by very-short-patch repair (VSP), while group-II tetramers are favored by VSP activity. The VSP system repairs G:T mismatches to G:C, thereby increasing the overall G+C content of the genome; for this reason the CTAG-rich sample has a lower G+C content than the CTAG-poor sample. This compositional heterogeneity can be tentatively explained by a low level of VSP activity on the CTAG-rich sample. A negative correlation is found between the frequency of group-I tetramers and the level of gene expression, as measured by the Codon Adaptation Index (CAI). A possible link between the rate of VSP activity and the level of gene expression is considered.Correspondence to: A. Marine 相似文献
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