Characterization of Two Dinoflagellate Cold Shock Domain Proteins

ABSTRACT Roughly two-thirds of the proteins annotated as transcription factors in dinoflagellate transcriptomes are cold shock domain-containing proteins (CSPs), an uncommon condition in eukaryotic organisms. However, no functional analysis has ever been reported for a dinoflagellate CSP, and so it...

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Autores principales:	Mathieu Beauchemin, Sougata Roy, Sarah Pelletier, Alexandra Averback, Frederic Lanthier, David Morse
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2016
Materias:	RNA binding domain DNA binding domain cold shock domain dinoflagellates cold shock protein transcription Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/18c2eaf3f3b64198b6b8436f6590be01
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spelling	oai:doaj.org-article:18c2eaf3f3b64198b6b8436f6590be012021-11-15T15:21:38ZCharacterization of Two Dinoflagellate Cold Shock Domain Proteins10.1128/mSphere.00034-152379-5042https://doaj.org/article/18c2eaf3f3b64198b6b8436f6590be012016-02-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00034-15https://doaj.org/toc/2379-5042ABSTRACT Roughly two-thirds of the proteins annotated as transcription factors in dinoflagellate transcriptomes are cold shock domain-containing proteins (CSPs), an uncommon condition in eukaryotic organisms. However, no functional analysis has ever been reported for a dinoflagellate CSP, and so it is not known if they do in fact act as transcription factors. We describe here some of the properties of two CSPs from the dinoflagellate Lingulodinium polyedrum, LpCSP1 and LpCSP2, which contain a glycine-rich C-terminal domain and an N-terminal cold shock domain phylogenetically related to those in bacteria. However, neither of the two LpCSPs act like the bacterial CSP, since they do not functionally complement the Escherichia coli quadruple cold shock domain protein mutant BX04, and cold shock does not induce LpCSP1 and LpCSP2 to detectable levels, based on two-dimensional gel electrophoresis. Both CSPs bind to RNA and single-stranded DNA in a nonspecific manner in electrophoretic mobility shift assays, and both proteins also bind double-stranded DNA nonspecifically, albeit more weakly. These CSPs are thus unlikely to act alone as sequence-specific transcription factors. IMPORTANCE Dinoflagellate transcriptomes contain cold shock domain proteins as the major component of the proteins annotated as transcription factors. We show here that the major family of cold shock domain proteins in the dinoflagellate Lingulodinium do not bind specific sequences, suggesting that transcriptional control is not a predominant mechanism for regulating gene expression in this group of protists.Mathieu BeaucheminSougata RoySarah PelletierAlexandra AverbackFrederic LanthierDavid MorseAmerican Society for MicrobiologyarticleRNA binding domainDNA binding domaincold shock domaindinoflagellatescold shock proteintranscriptionMicrobiologyQR1-502ENmSphere, Vol 1, Iss 1 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	RNA binding domain DNA binding domain cold shock domain dinoflagellates cold shock protein transcription Microbiology QR1-502
spellingShingle	RNA binding domain DNA binding domain cold shock domain dinoflagellates cold shock protein transcription Microbiology QR1-502 Mathieu Beauchemin Sougata Roy Sarah Pelletier Alexandra Averback Frederic Lanthier David Morse Characterization of Two Dinoflagellate Cold Shock Domain Proteins
description	ABSTRACT Roughly two-thirds of the proteins annotated as transcription factors in dinoflagellate transcriptomes are cold shock domain-containing proteins (CSPs), an uncommon condition in eukaryotic organisms. However, no functional analysis has ever been reported for a dinoflagellate CSP, and so it is not known if they do in fact act as transcription factors. We describe here some of the properties of two CSPs from the dinoflagellate Lingulodinium polyedrum, LpCSP1 and LpCSP2, which contain a glycine-rich C-terminal domain and an N-terminal cold shock domain phylogenetically related to those in bacteria. However, neither of the two LpCSPs act like the bacterial CSP, since they do not functionally complement the Escherichia coli quadruple cold shock domain protein mutant BX04, and cold shock does not induce LpCSP1 and LpCSP2 to detectable levels, based on two-dimensional gel electrophoresis. Both CSPs bind to RNA and single-stranded DNA in a nonspecific manner in electrophoretic mobility shift assays, and both proteins also bind double-stranded DNA nonspecifically, albeit more weakly. These CSPs are thus unlikely to act alone as sequence-specific transcription factors. IMPORTANCE Dinoflagellate transcriptomes contain cold shock domain proteins as the major component of the proteins annotated as transcription factors. We show here that the major family of cold shock domain proteins in the dinoflagellate Lingulodinium do not bind specific sequences, suggesting that transcriptional control is not a predominant mechanism for regulating gene expression in this group of protists.
format	article
author	Mathieu Beauchemin Sougata Roy Sarah Pelletier Alexandra Averback Frederic Lanthier David Morse
author_facet	Mathieu Beauchemin Sougata Roy Sarah Pelletier Alexandra Averback Frederic Lanthier David Morse
author_sort	Mathieu Beauchemin
title	Characterization of Two Dinoflagellate Cold Shock Domain Proteins
title_short	Characterization of Two Dinoflagellate Cold Shock Domain Proteins
title_full	Characterization of Two Dinoflagellate Cold Shock Domain Proteins
title_fullStr	Characterization of Two Dinoflagellate Cold Shock Domain Proteins
title_full_unstemmed	Characterization of Two Dinoflagellate Cold Shock Domain Proteins
title_sort	characterization of two dinoflagellate cold shock domain proteins
publisher	American Society for Microbiology
publishDate	2016
url	https://doaj.org/article/18c2eaf3f3b64198b6b8436f6590be01
work_keys_str_mv	AT mathieubeauchemin characterizationoftwodinoflagellatecoldshockdomainproteins AT sougataroy characterizationoftwodinoflagellatecoldshockdomainproteins AT sarahpelletier characterizationoftwodinoflagellatecoldshockdomainproteins AT alexandraaverback characterizationoftwodinoflagellatecoldshockdomainproteins AT fredericlanthier characterizationoftwodinoflagellatecoldshockdomainproteins AT davidmorse characterizationoftwodinoflagellatecoldshockdomainproteins
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Characterization of Two Dinoflagellate Cold Shock Domain Proteins

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