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Heqiao Zhang Dong-Hua Chen Rayees U.H. Mattoo David A. Bushnell Yannan Wang Chao Yuan Lin Wang Chunnian Wang Ralph E. Davis Yan Nie Roger D. Kornberg 《Molecular cell》2021,81(8):1781-1788.e4
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Yan-Hong He Guo-Gui Ning Ya-Lin Sun Yan Hu Xing-Yu Zhao Man-Zhu Bao 《Molecular breeding : new strategies in plant improvement》2010,26(1):19-29
A male sterile line was isolated in marigold (Tagetes erecta L.) and cytological analysis determined this to be a novel genic male sterility trait (Tems). Through the use of amplified fragment length polymorphisms (AFLPs) and bulked segregant analysis (BSA), tightly linked
markers of Tems were identified with a view towards a map-based cloning strategy. It was found that spontaneous homeotic conversion of floral
organs was the underlying cause of the male sterility in this marigold line. Thus, petals of male sterile plants resembled
sepal-like structures and the stamens were partially converted to styles, although without the full characteristics or function
of the true style organs. We have constructed a fine marker-based map for the Tems gene. This is intended to provide a tool for marker assisted selection (MAS) strategies in hybrid breeding and map-based
cloning strategies for the male sterility locus. We discuss the significance of this spontaneously derived genic male sterility
trait relating to the homeotic conversion of floral organs in marigold. 相似文献
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Abstract Rheocricotopus (Psilocricotopus) taiwanensis sp. n. from Taiwan, China, is described as male imagines. The species is allied to R. (P.) chalybeatus (Edwards) but it is easily separated from the latter in lacking setae in all reins, much lower AR and more pronounced crista dorsalis in gonostylus. The genus is new to Taiwan Province, China. The specimen is deposited at the Department of Biology, Nankai University, Tianjin. 相似文献
39.
Yan Yongshan Fen Shang Liu Lianrui 《TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik》1987,74(1):147-153
Summary A 8.3 /ml 6-thioguanine (6TG)-resistant strain was isolated from a rat tetraploid cell line by step-by-step selection in 6TG-medium. In the 6TG-resistant cell population 51% of the cells were tetraploid and 35% of the cells were hypertetraploid, i.e., one chromosome more than a tetraploid. The 6TG-resistant strain grew very well in RPMI 1640 medium with intervals of three days between subcultures. The 6TG-resistant cells all have a homogeneously staining region (HSRs) in one of the X chromosomes which do not stain after chromosome C-banding. They also possess a higher NORs activity and much lower frequency of sister chromatid exchanges (SCE). When the 6TG-resistant RCT cells were subcultured in 6TG-free medium for three days, their SCE frequency did not change. 5-bromodeoxyuridine (BrdU) significantly suppressed the NORs activity for both 6TG-resistant cells and 6TG-sensitive cells (P<0.001).Abbreviations 6TG
6-thioguanine
- HSRs
homogeneously staining region
- NORs
nucleolar organizer region
- SCE
sister chromatid exchange
- BrdU
5-bromodeoxyuridine
- HPRT
Hypoxanthine phosphoribosyl transferase 相似文献
40.
Purification and Characterization of a Substrate-Size-Recognizing Metalloendopeptidase from Streptococcus cremoris H61 总被引:6,自引:5,他引:1
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Tsong-Rong Yan Norihiro Azuma Shuichi Kaminogawa Kunio Yamauchi 《Applied microbiology》1987,53(10):2296-2302
During the ripening of Gouda-type cheese, two kinds of endopeptidases were found to participate in the degradation of αs1-CN(f1-23), a specific product from αs1-casein hydrolyzed by chymosin. One of the endopeptidases, lactic acid bacteria endopeptidase (LEP-II), which can recognize the size of its substrates, has already been purified and characterized (T. R. Yan, N. Azuma, S. Kaminogawa, and K. Yamauchi, Eur. J. Biochem. 163:259-265, 1987). The other endopeptidase, LEP-I, was purified to homogeneity by conventional chromatographic techniques from Streptococcus cremoris H61. The enzyme appeared to be monomeric, with an apparent molecular weight of 98,000, and its isoelectric point was 5.1. For the hydrolysis of αs1-CN(f1-23), the enzyme had an optimum pH and temperature of 7.0 to 7.5 and 40°C, respectively. Its activity was inhibited by such chelating agents as EDTA and 1,10-phenanthrolin, and it could be fully reactivated by Mn2+. Inhibitors specific for serine and thiol proteases had no effect on the protease activity. The enzyme showed a high affinity toward the Glu-Asn peptide bond of αs1-CN(f1-23) and αs1-CN(f91-100) but showed no hydrolysis activity toward αs1-CN(f1-52), αs1-CN(61-122), αs1-CN(136-196), αs1-casein, β-casein, κ-casein, α-lactalbumin, and β-lactoglobulin. The Km and Vmax of LEP-I for αs1-CN(f1-23) were 14.2 pM and 139 U, respectively. 相似文献