Please do not adjust margins
ChemComm
Page 4 of 4
COMMUNICATION
Journal Name
11.
S. Singh, D. Padovani, R. A. Leslie, T. Chiku and R.
Banerjee, The Journal of biologicaDl cOhI:e1m0.i1s0tr3y9,/2C090C9C,02380420, D
22457-22466.
forming Cys persulfides from H2S and behaving similarly to
mammalian 3MST.16 Based on this information, deletion of
TUM1 was expected to result in a reduction of Cys persulfides
derived from Cys. However, the presence of TUM1, not its
absence, appears to be correlated with a decrease in all
polysulfide species. For example, the Δtum1 mutant displayed
larger peak areas for GSSH and GSSG in SO42- and Cys compared
to BY4743. This could be due to increased Cys leading to
increased GSH, hence the ability to form more GSH-derived
polysulfides. It is also noteworthy that CysSSH was produced
only from Cys in Δtum1 cells. Therefore, cells can still produce
CysSSH from Cys without a functional Tum1p enzyme, meaning
there could be other yeast genes capable of producing CysSSH
from Cys.
This study has shown for the first time the occurrence and
biosynthesis of polysulfides in yeast. Using a novel synthetic
approach to prepare specific polysulfides in combination with
LC-MS/MS methodology we have shown the viability of using
yeast as a model system for complex semi-quantitative
polysulfidomics. Furthermore, we have provided evidence that
altering the sulfur source for yeast growth alters the polysulfide
content and started to unravel the roles of Sc genes in
polysulfide biosynthesis.
12.
13.
14.
R. Miyamoto, K. I. Otsuguro, S. Yamaguchi and S. Ito,
Journal of Neurochemistry, 2014, 130, 29-40.
K. Kashfi and K. R. Olson, Biochemical Pharmacology,
2013, 85, 689-703.
M. I. Kinzurik, K. Ly, K. M. David, R. C. Gardner and B.
Fedrizzi, ACS Chemical Biology, 2017, 12, 414-421.
M. Santiago and R. C. Gardner, Yeast, 2015, 32, 519-532.
C. W. Huang, M. E. Walker, B. Fedrizzi, M. Roncoroni, R. C.
Gardner and V. Jiranek, FEMS Yeast Research, 2016, 16.
C. W. Huang, M. E. Walker, B. Fedrizzi, R. C. Gardner and
V. Jiranek, FEMS Yeast Research, 2017, 17.
D. J. Smith and V. Venkatraghavan, Synthetic
Communications, 1985, 15, 945-950.
M. M. Cerda, M. D. Hammers, M. S. Earp, L. N. Zakharov
and M. D. Pluth, Organic Letters, 2017, 19, 2314-2317.
G. L. Newton, R. Dorian and R. C. Fahey, Analytical
Biochemistry, 1981, 114, 383-387.
W. Chen, C. Liu, B. Peng, Y. Zhao, A. Pacheco and M. Xian,
Chemical Science, 2013, 4, 2892-2896.
E. Marutani, M. Sakaguchi, W. Chen, K. Sasakura, J. Liu, M.
Xian, K. Hanaoka, T. Nagano and F. Ichinose,
MedChemComm, 2014, 5, 1577-1583.
F. Yu, X. Han and L. Chen, Chemical Communications,
2014, 50, 12234-12249.
J. A. Jastrzembski, R. B. Allison, E. Friedberg and G. L.
Sacks, Journal of Agricultural and Food Chemistry, 2017,
65, 10542-10549.
M. Fauchon, G. Lagniel, J. C. Aude, L. Lombardia, P.
Soularue, C. Petat, G. Marguerie, A. Sentenac, M. Werner
and J. Labarre, Molecular Cell, 2002, 9, 713-723.
T. Drakulic, M. D. Temple, R. Guido, S. Jarolim, M.
Breitenbach, P. V. Attfield and I. W. Dawes, FEMS Yeast
Research, 2005, 5, 1215-1228.
15.
16.
17.
18.
19.
20.
21.
22.
23.
24.
Acknowledgements
We thank the Faculty Research and Development Fund from
The University of Auckland for supporting this research.
25.
26.
Conflicts of interest
There are no conflicts to declare.
27.
28.
29.
G. Powis, M. Briehl and J. Oblong, Pharmacology and
Therapeutics, 1995, 68, 149-173.
S. Yamagata, R. J. D'Andrea, S. Fujisaki, M. Isaji and K.
Nakamura, Journal of Bacteriology, 1993, 175, 4800-4808.
H. Kunikata, T. Ida, K. Sato, N. Aizawa, T. Sawa, H.
Tawarayama, N. Murayama, S. Fujii, T. Akaike and T.
Nakazawa, Scientific Reports, 2017, 7.
A. Noma, Y. Sakaguchi and T. Suzuki, Nucleic Acids
Research, 2009, 37, 1335-1352.
S. Leidel, P. G. A. Pedrioli, T. Bucher, R. Brost, M.
Costanzo, A. Schmidt, R. Aebersold, C. Boone, K. Hofmann
and M. Peter, Nature, 2009, 458, 228-232.
Notes and references
1.
2.
N. Sen, Journal of Molecular Biology, 2017, 429, 543-561.
M. M. Gadalla and S. H. Snyder, Journal of
Neurochemistry, 2010, 113, 14-26.
3.
4.
L. Li, P. Rose and P. K. Moore, Journal, 2011, 51, 169-187.
R. Wang, Antioxidants and Redox Signaling, 2003, 5, 493-
501.
30.
31.
5.
6.
7.
8.
H. Kimura, Antioxidants & redox signaling, 2015, 22, 362-
376.
C. Jacob, A. Anwar and T. Burkholz, Planta Medica, 2008,
74, 1580-1592.
T. V. Mishanina, M. Libiad and R. Banerjee, Nature
Chemical Biology, 2015, 11, 457-464.
T. Ida, T. Sawa, H. Ihara, Y. Tsuchiya, Y. Watanabe, Y.
Kumagai, M. Suematsu, H. Motohashi, S. Fujii, T.
Matsunaga, M. Yamamoto, K. Ono, N. O. Devarie-Baez, M.
Xian, J. M. Fukuto and T. Akaike, Proceedings of the
National Academy of Sciences of the United States of
America, 2014, 111, 7606-7611.
9.
H. Kimura, Antioxidants and Redox Signaling, 2014, 20,
783-793.
10.
N. Lau and M. D. Pluth, Current Opinion in Chemical
Biology, 2019, 49, 1-8.
4 | J. Name., 2012, 00, 1-3
This journal is © The Royal Society of Chemistry 20xx
Please do not adjust margins