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1.
iScience ; 26(3): 106168, 2023 Mar 17.
Article in English | MEDLINE | ID: mdl-36876122

ABSTRACT

Marine organisms living at high latitudes are faced with a light climate that undergoes drastic annual changes, especially during the polar night (PN) when the sun remains below the horizon for months. This raises the question of a possible synchronization and entrainment of biological rhythms under the governance of light at very low intensities. We analyzed the rhythms of the mussel Mytilus sp. during PN. We show that (1) mussels expressed a rhythmic behavior during PN; (2) a monthly moonlight rhythm was expressed; (3) a daily rhythm was expressed and influenced by both sunlight and moonlight; and (4) depending on the different times of PN and moon cycle characteristics, we were able to discriminate whether the moon or the sun synchronize the daily rhythm. Our findings fuel the idea that the capability of moonlight to synchronize daily rhythms when sunlight is not sufficient would be a crucial advantage during PN.

2.
R Soc Open Sci ; 7(10): 200889, 2020 Oct.
Article in English | MEDLINE | ID: mdl-33204461

ABSTRACT

Polar regions are currently warming at a rate above the global average. One issue of concern is the consequences on biodiversity in relation to the Northward latitudinal shift in distribution of temperate species. In the present study, lasting almost two years, we examined two phenological traits, i.e. the shell growth and behavioural rhythm of a recently re-established species in the high Arctic, the blue mussel Mytilus sp. We compared this with a native species, the Islandic scallop Chlamys islandica. We show marked differences in the examined traits between the two species. In Mytilus sp., a clear annual pattern of shell growth strongly correlated to the valve behaviour rhythmicity, whereas C. islandica exhibited a shell growth pattern with a total absence of annual rhythmicity of behaviour. The shell growth was highly correlated to the photoperiod for the mussels but weaker for the scallops. The water temperature cycle was a very weak parameter to anticipate the phenology traits of both species. This study shows that the new resident in the high Arctic, Mytilus sp., is a highly adaptive species, and therefore a promising bioindicator to study the consequences of biodiversity changes due to global warming.

3.
Evol Appl ; 10(1): 39-55, 2017 01.
Article in English | MEDLINE | ID: mdl-28035234

ABSTRACT

Climate changes in the Arctic are predicted to alter distributions of marine species. However, such changes are difficult to quantify because information on present species distribution and the genetic variation within species is lacking or poorly examined. Blue mussels, Mytilus spp., are ecosystem engineers in the coastal zone globally. To improve knowledge of distribution and genetic structure of the Mytilus edulis complex in the Arctic, we analyzed 81 SNPs in 534 Mytilus spp. individuals sampled at 13 sites to provide baseline data for distribution and genetic variation of Mytilus mussels in the European Arctic. Mytilus edulis was the most abundant species found with a clear genetic split between populations in Greenland and the Eastern Atlantic. Surprisingly, analyses revealed the presence of Mytilus trossulus in high Arctic NW Greenland (77°N) and Mytilus galloprovincialis or their hybrids in SW Greenland, Svalbard, and the Pechora Sea. Furthermore, a high degree of hybridization and introgression between species was observed. Our study highlights the importance of distinguishing between congener species, which can display local adaptation and suggests that information on dispersal routes and barriers is essential for accurate predictions of regional susceptibility to range expansions or invasions of boreal species in the Arctic.

4.
Proteomics ; 13(16): 2386-97, 2013 Aug.
Article in English | MEDLINE | ID: mdl-23733317

ABSTRACT

Chromatographed peptide signals form the basis of further data processing that eventually results in functional information derived from data-dependent bottom-up proteomics assays. We seek to rank LC/MS parent ions by the quality of their extracted ion chromatograms. Ranked extracted ion chromatograms act as an intuitive physical/chemical preselection filter to improve the quality of MS/MS fragment scans submitted for database search. We identify more than 4900 proteins when considering detector shifts of less than 7 ppm. High quality parent ions for which the database search yields no hits become candidates for subsequent unrestricted analysis for PTMs. Following this rational approach, we prioritize identification of more than 5000 spectrum matches from modified peptides and confirmed the presence of acetylaldehyde-modified His/Lys. We present a logical workflow that scores data-dependent selected ion chromatograms and leverage information about semianalytical LC/LC dimension prior to MS. Our method can be successfully used to identify unexpected modifications in peptides with excellent chromatography characteristics, independent of fragmentation pattern and activation methods. We illustrate analysis of ion chromatograms detected in two different modes by RF linear ion trap and electrostatic field orbitrap.


Subject(s)
Peptides/analysis , Peptides/chemistry , Proteomics/methods , Software , Tandem Mass Spectrometry/methods , Databases, Protein , HEK293 Cells , Humans , Models, Statistical
5.
J Am Soc Mass Spectrom ; 24(8): 1315-8, 2013 Aug.
Article in English | MEDLINE | ID: mdl-23740032

ABSTRACT

With the development of new synthesis procedures, an ever increasing number of chemical modifications can now be incorporated into synthetic oligonucleotides, representing new challenges for analytical chemists to efficiently identify and characterize such molecules. While conventional mass spectrometry (MS) has proven to be a powerful tool to study nucleic acids, new and improved methods and software are now needed to address this emerging challenge. In this report, we describe a simple yet powerful program that affords great flexibility in the calculation of theoretical masses for conventional as well as modified oligonucleotide molecules. This easy to use program can accept input oligonucleotide sequences and then calculate the theoretical mass values for full length products, process impurities, potential metabolites, and gas phase fragments. We intentionally designed this software so that modified nucleotide residues can be incorporated into oligonucleotide sequences, and corresponding mass values can be rapidly calculated. To test the utility of this program, two oligonucleotides that contain a large number of chemical modifications were synthesized. We have analyzed these samples using a Q-TOF mass spectrometer and compared the calculated masses to the observed ones. We found that all of the data matched very well with less than 30 ppm mass errors, well within the expectation for our instrument operated in its current mode. These data confirmed the validity of calculations performed with this new software.


Subject(s)
Oligonucleotides/chemistry , Chromatography, High Pressure Liquid , Enzymes/chemistry , Mass Spectrometry , Molecular Weight , Oligonucleotides/chemical synthesis , Phosphates/analysis , Spectrophotometry, Ultraviolet
7.
Electrophoresis ; 26(1): 248-56, 2005 Jan.
Article in English | MEDLINE | ID: mdl-15624161

ABSTRACT

Intact protein masses from immortal, nontransformed MCF10A, a human breast epithelial cell line, and its malignant derivative MCF10CA1a.cl1 have been mapped using a combination of all-liquid separations and automated data interpretation. Preparative liquid isoelectric focusing combined with nonporous silica reverse-phase high-performance liquid chromatography allows efficient separation of a large number of proteins in complex mixtures such as whole-cell lysates. Molecular weight determination of these proteins is achieved using electrospray-time of flight-mass spectrometry, however, manual data analysis for these separations is both complex and time-consuming. Protein mass mapping can be significantly enhanced by automating deconvolution functions typically performed manually, with resulting reductions in hands-on analysis time from 20-30 h per chromatogram to approximately 15 min. This reduction in analysis time allows for rapid screening of cancer cell lines for potential biomarkers over a wider pI range than would otherwise be possible.


Subject(s)
Biomarkers, Tumor/analysis , Breast Neoplasms/chemistry , Neoplasm Proteins/analysis , Spectrometry, Mass, Electrospray Ionization/methods , Biomarkers, Tumor/isolation & purification , Cell Extracts/chemistry , Cell Line, Tumor , Chromatography, High Pressure Liquid , Female , Humans , Isoelectric Focusing , Molecular Weight , Neoplasm Proteins/isolation & purification
9.
Anal Chem ; 74(22): 5807-13, 2002 Nov 15.
Article in English | MEDLINE | ID: mdl-12463365

ABSTRACT

We describe an integrated approach for automating protein analysis of bacterial cell extracts. The method uses electrospray LC/MS to generate chromatographic profiles of proteins present in an extract, along with a software program that automates the data analysis. The software program, Retana, automates the sequential summing, centroiding, and deconvolution of multiply charged proteins present in consecutive scans of the LC/MS analysis. This procedure generates a concise, single spectrum of proteins present in the extract, along with their retention time and relative abundance. A comparison of the method with "whole cell" MALDI analysis demonstrates improved mass resolution and mass accuracy, along with the appearance of a greater number of proteins. Additionally, it is possible to compare protein expression among strains of bacteria by normalizing the relative abundance of similar proteins in each analysis.


Subject(s)
Bacterial Proteins/biosynthesis , Bacterial Proteins/chemistry , Automation , Chromatography, High Pressure Liquid , Data Interpretation, Statistical , Protein Processing, Post-Translational , Spectrometry, Mass, Electrospray Ionization , Vibrio parahaemolyticus/chemistry , Vibrio parahaemolyticus/metabolism
10.
J Microbiol Methods ; 48(2-3): 107-15, 2002 Feb.
Article in English | MEDLINE | ID: mdl-11777561

ABSTRACT

A new sample preparation method was developed for fresh, whole-cell Gram-positive bacteria to be analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI ToF MS). With fresh, whole-cell Gram-negative bacteria of the Enterobacteriaceae family, we had previously achieved spectra consisting of >50 peaks and mass ranges of 2-25 kDa. Because similar spectral quantity could not be achieved for Gram-positive bacteria, using this same protocol, we investigated an alternative approach that focuses on the thick peptidoglycan layer of the cell wall. Gram-positive bacteria were incubated with 0.05-0.5 mg/ml lysozyme for 30 min prior to being analyzed by MALDI ToF MS. Lysozyme is an enzymatically stable, 14-kDa protein that specifically cleaves between peptidoglycan disaccharide subunits. A significant increase in overall number of peaks (>50) in the 2-14 kDa range was observed without interference from the presence of lysozyme. We show that for four different species (Staphylococcus aureus, S. haemolyticus, Streptococcus pyogenes, and S. agalactiae) reproducible subset of peaks were found within spectra from a reference strain and two unrelated clinical isolates. The data suggests that this sample preparation may be useful for increasing the overall number of peaks within spectra for subsequent development of bacterial identification strategies.


Subject(s)
Gram-Positive Bacteria/chemistry , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Biomarkers , Gram-Positive Bacteria/isolation & purification , Gram-Positive Bacteria/physiology , Reproducibility of Results
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