Proteomics & Metabolomics
In addition to doing work on existing IGBB projects, the IGBB proteomics staff can
perform a variety of mass spectrometry and other proteomics services for MS State principal investigators and
IGBB collaborators. Such research can be performed through a Proposal Partnership,
a Research Agreement, or the Service Center.
The
IGBB's proteomics staff has considerable expertise in...
- Protein isolation/purification from all types of organisms/tissues
- 1D & 2D gel electrophoresis
- Gel- and non-gel-based mass spectrometry
- Protein identification
- Discovery and characterization of post-translational modifications;
- Quantitative proteomics
- Comparative proteomics & metabolomics
- Western blotting & protein visualization
- Integration of proteomic and nucleic acids data (e.g., proteogenomic
mapping)
- Functional annotation of proteins using Gene Ontology (GO)
standards and procedures
With regard to mass spectrometers, the IGBB's proteomics staff utilizes a ThermoFisher LTQ Orbitrap Velos, a Waters Nano ESI Q-TOF (model Xevo G2-S), and an Applied Biosystems (now ThermoFisher) MALDI TOF TOF. The LTQ Orbitrap Velos and the Nano ESI Q-TOF are fitted with upstream HPLC sample
purification systems.
To discuss the possibility of having the IGBB conduct
proteomics research in collaboration with you, please submit a ticket through the MyIGBB HelpDesk.
An IGBB proteomics consultant will respond to your query as quickly as possible
(usually within 24 hours).
A listing of IGBB Standard Services and their prices -- including information and prices for Training and Self-Service Equipment Usage -- is available in the Standard Services Catalog in MyIGBB and in PDF form via the link below.
ALSO SEE: Genomics (including Transcriptomics) | Biocomputing (Bioinformatics & Computational Biology)
NOTE: PIs are asked to consider whether the participation of an IGBB employee in a project merits that employee's inclusion as a co-author on a resulting manuscript(s). The decision ultimately lies with the PI. However, the IGBB encourages IGBB staff and faculty involved in
Proposal Partnerships and
Research Agreements to discuss/negotiate co-authorship with PIs before starting work on a project.
Diane GodwinPublications Manager
GRAPHIC DESIGN
email(662) 325-9333
Portera
Phylogenomics demonstrates that breviate flagellates are related to opisthokonts and apusomonads
IGBB Authors:
Matthew W. BrownPUBLICATION YEAR:
2013IMPACT FACTOR:
5.843CITATION COUNT:
113Brown MW, Sharpe SC, Silberman JD, Heiss AA, Lang BF, Simpson AG,Roger AJ (2013) Phylogenomics demonstrates that breviate flagellates are related to opisthokonts and apusomonads.
Proceedings of the Royal Society B: Biological Sciences 280(1769): 20131755.
DOI:
10.1098/rspb.2013.1755EID:
2-s2.0-84892577995PMID: 23986111
DOWNLOAD PDFABSTRACTMost eukaryotic lineages belong to one of a few major groups. However, several protistan lineages have not yet been robustly placed in any of these groups. Both the breviates and apusomonads are two such lineages that appear to be related to the Amoebozoa and Opisthokonta (i.e. the 'unikonts' or Amorphea); however, their precise phylogenetic positions remain unclear. Here, we describe a novel microaerophilic breviate, Pygsuia biforma gen. nov. sp. nov., isolated from a hypoxic estuarine sediment. Ultrastructurally, this species resembles the breviate genera Breviata and Subulatomonas but has two cell morphologies, adherent and swimming. Phylogenetic analyses of the small sub-unit rRNA gene show that Pygsuia is the sister to the other breviates. We constructed a 159-protein supermatrix, including orthologues identified in RNA-seq data from Pygsuia. Phylogenomic analyses of this dataset show that breviates, apusomonads and Opisthokonta form a strongly supported major eukaryotic grouping we name the Obazoa. Although some phylogenetic methods disagree, the balance of evidence suggests that the breviate lineage forms the deepest branch within Obazoa. We also found transcripts encoding a nearly complete integrin adhesome from Pygsuia, indicating that this protein complex involved in metazoan multicellularity may have evolved earlier in eukaryote evolution than previously thought.
The IGBB is supported, in part, by the following units:
The IGBB is an HPC² member center.
