• Title/Summary/Keyword: Ycs4

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Ycs4 is Required for Efficient Double-Strand Break Formation and Homologous Recombination During Meiosis

  • Hong, Soogil;Choi, Eui-Hwan;Kim, Keun Pil
    • Journal of Microbiology and Biotechnology
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    • v.25 no.7
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    • pp.1026-1035
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    • 2015
  • Condensin is not only responsible for chromosome condensation, but is also involved in double-strand break (DSB) processing in the cell cycle. During meiosis, the condensin complex serves as a component of the meiotic chromosome axis, and mediates both proper assembly of the synaptonemal complex and DSB repair, in order to ensure proper homologous chromosome segregation. Here, we used the budding yeast Saccharomyces cerevisiae to show that condensin participates in a variety of chromosome organization processes and exhibits crucial molecular functions that contribute to meiotic recombination during meiotic prophase I. We demonstrate that Ycs4 is required for efficient DSB formation and establishing homolog bias at the early stage of meiotic prophase I, which allows efficient formation of interhomolog recombination products. In the Ycs4 meiosis-specific allele (ycs4S), interhomolog products were formed at substantial levels, but with the same reduction in crossovers and noncrossovers. We further show that, in prophase chromosomal events, ycs4S relieved the defects in the progression of recombination interactions induced as a result of the absence of Rec8. These results suggest that condensin is a crucial coordinator of the recombination process and chromosome organization during meiosis.

Effects of yeast culture (Saccharomyces cerevisiae) supplementation on growth performance, fecal score, and nutrient digestibility of weaning pigs

  • Liu, Xiao;Li, Tianshui;Kim, In Ho
    • Korean Journal of Agricultural Science
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    • v.45 no.4
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    • pp.677-685
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    • 2018
  • Weaning pigs often face post-weaning challenges such as diarrhea, low feed intake, and body weight (BW) loss which affects the health and economic value of weaning pigs. Interestingly, the use of yeast cultures (YCs) as feed supplements for pigs has increased markedly in recent years. This study evaluated the effects of yeast cultures (Saccharomyces cerevisiae) on the growth performance, fecal score, and nutrient digestibility of weaning pigs. A total of 50 crossed healthy weaning pigs [(Yorkshire ${\times}$ Landrace) ${\times}$ Duroc] with an average BW of $7.46{\pm}1.60kg$ (28 day of age) were used in a 6-week experiment. The experiment was divided into 3 phases (Phase 1, 1 - 2 weeks; Phase 2, 2 - 4 weeks; Phase 3, 4 - 6 weeks). Dietary treatments were as follows: 1) CON: basal diet and 2) CON + 0.50% YC. During phase 1, the average daily gain (ADG) and average daily feed intake (ADFI) were significantly increased (p < 0.05) in the weaning pigs fed YC supplementation diets compared with the weaning pigs fed the CON diet. During phase 3 as well as overall, the gain/feed ratio (G/F) was significantly increased (p < 0.05) in the YC supplementation group compared with the pigs fed the CON diet. In conclusion, the supplementation of YCs in the diet positively affected the growth performance of weaning pigs during the first two weeks after weaning.

Genetic Structure of the phnM Gene Encoding Plant-Type Ferredoxin from Pseudomonas sp. strain DJ77 (Pseudomonas sp. strain DJ77에서 Plant-Type의 Ferredoxin을 암호화하는 phnM 유전자의 구조)

  • Kim, Sungje;Kim, Young-Chang
    • Korean Journal of Microbiology
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    • v.34 no.3
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    • pp.115-119
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    • 1998
  • We cloned the 4.8 kb BglII fragment containing genes downstream pHENX7 from Pseudomonas sp. strain DJ77. The restriction map of the resultant clone, recombinant plasmid pYCS500, was determined. Sequencing analysis of the 465 bp HindIII-ClaI fragment revealed an open reading frame of 282 bp that was then designated phnM. The deduced polypeptide is 93 amino acid residues long with a $M_r$ of 10,008. The PhnM has 37.3-53.9% identity with plant-type ferredoxin proteins such as NahT, XylT, DmpQ, AtdS, PhlG, PhhQ and TbuW and contains the motif similar to well-conserved functional domains of those proteins.

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