PMID- 21143936
OWN - NLM
STAT- MEDLINE
DCOM- 20110223
LR  - 20211020
IS  - 1471-2180 (Electronic)
IS  - 1471-2180 (Linking)
VI  - 10
DP  - 2010 Dec 9
TI  - Interaction of the heterotrimeric G protein alpha subunit SSG-1 of Sporothrix 
      schenckii with proteins related to stress response and fungal pathogenicity using 
      a yeast two-hybrid assay.
PG  - 317
LID - 10.1186/1471-2180-10-317 [doi]
AB  - BACKGROUND: Important biological processes require selective and orderly 
      protein-protein interactions at every level of the signalling cascades. G 
      proteins are a family of heterotrimeric GTPases that effect eukaryotic signal 
      transduction through the coupling of cell surface receptors to cytoplasmic 
      effector proteins. They have been associated with growth and pathogenicity in 
      many fungi through gene knock-out studies. In Sporothrix schenckii, a pathogenic, 
      dimorphic fungus, we previously identified a pertussis sensitive G alpha subunit, 
      SSG-1. In this work we inquire into its interactions with other proteins. 
      RESULTS: Using the yeast two-hybrid technique, we identified protein-protein 
      interactions between SSG-1 and other important cellular proteins. The 
      interactions were corroborated using co-immuneprecipitation. Using these 
      techniques we identified a Fe/Mn superoxide dismutase (SOD), a glyceraldehyde-3-P 
      dehydrogenase (GAPDH) and two ion transport proteins, a siderophore-iron 
      transporter belonging to the Major Facilitator Superfamily (MFS) and a 
      divalent-cation transporter of the Nramp (natural resistance-associated 
      macrophage protein) family as interacting with SSG-1. The cDNA's encoding these 
      proteins were sequenced and bioinformatic macromolecular sequence analyses were 
      used for the correct classification and functional assignment. CONCLUSIONS: This 
      study constitutes the first report of the interaction of a fungal G alpha 
      inhibitory subunit with SOD, GAPDH, and two metal ion transporters. The 
      identification of such important proteins as partners of a G alpha subunit in 
      this fungus suggests possible mechanisms through which this G protein can affect 
      pathogenicity and survival under conditions of environmental stress or inside the 
      human host. The two ion transporters identified in this work are the first to be 
      reported in S. schenckii and the first time they are identified as interacting 
      with fungal G protein alpha subunits. The association of G protein alpha subunits 
      to transport molecules reinforces the role of G proteins in the response to 
      environmental signals and also highlights the involvement of fungal G protein 
      alpha subunits in nutrient sensing in S. schenckii. These interactions suggest 
      that these permeases could function as transceptors for G proteins in fungi.
FAU - Perez-Sanchez, Lizaida
AU  - Perez-Sanchez L
AD  - Department of Microbiology and Medical Zoology, Medical Sciences Campus, 
      University of Puerto Rico, PO Box 365067, San Juan, PR 00936-5067, USA.
FAU - Gonzalez, Elizabeth
AU  - Gonzalez E
FAU - Colon-Lorenzo, Emilee E
AU  - Colon-Lorenzo EE
FAU - Gonzalez-Velazquez, Waleska
AU  - Gonzalez-Velazquez W
FAU - Gonzalez-Mendez, Ricardo
AU  - Gonzalez-Mendez R
FAU - Rodriguez-del Valle, Nuri
AU  - Rodriguez-del Valle N
LA  - eng
GR  - 2 P41 RR06009-16A1/RR/NCRR NIH HHS/United States
GR  - 3S06-GM-008224/GM/NIGMS NIH HHS/United States
GR  - R25GM061838/GM/NIGMS NIH HHS/United States
GR  - T36GM008789-05/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20101209
PL  - England
TA  - BMC Microbiol
JT  - BMC microbiology
JID - 100966981
RN  - 0 (Fungal Proteins)
RN  - 0 (GTP-Binding Protein alpha Subunits)
RN  - 0 (Peptide Fragments)
RN  - 130349-12-1 (glyceraldehyde 3-phosphate dehydrogenase (304-313))
RN  - EC 1.15.1.1 (Superoxide Dismutase)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
SB  - IM
EIN - BMC Microbiol. 2019 Nov 26;19(1):262. PMID: 31771508
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Fungal Proteins/chemistry/genetics/*metabolism
MH  - GTP-Binding Protein alpha Subunits/chemistry/genetics/*metabolism
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/genetics/metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Peptide Fragments/genetics/metabolism
MH  - Protein Binding
MH  - Protein Multimerization
MH  - Sporothrix/chemistry/genetics/pathogenicity/*physiology
MH  - Sporotrichosis/microbiology
MH  - Stress, Physiological
MH  - Superoxide Dismutase/genetics/metabolism
MH  - Two-Hybrid System Techniques
PMC - PMC3018405
EDAT- 2010/12/15 06:00
MHDA- 2011/02/24 06:00
PMCR- 2010/12/09
CRDT- 2010/12/15 06:00
PHST- 2010/08/13 00:00 [received]
PHST- 2010/12/09 00:00 [accepted]
PHST- 2010/12/15 06:00 [entrez]
PHST- 2010/12/15 06:00 [pubmed]
PHST- 2011/02/24 06:00 [medline]
PHST- 2010/12/09 00:00 [pmc-release]
AID - 1471-2180-10-317 [pii]
AID - 10.1186/1471-2180-10-317 [doi]
PST - epublish
SO  - BMC Microbiol. 2010 Dec 9;10:317. doi: 10.1186/1471-2180-10-317.