BHLH - Revision history

Xysj2012: /* Brief Introduction */

2013-07-21T12:47:14Z

‎Brief Introduction

Xysj2012: /* Brief Introduction */

2013-07-21T12:31:12Z

‎Brief Introduction

Xysj2012 at 12:28, 21 July 2013

2013-07-21T12:28:03Z

Xysj2012: /* Brief Introduction */

2013-07-13T05:32:59Z

‎Brief Introduction

Xysj2012: /* Brief Introduction */

2013-07-13T05:32:24Z

‎Brief Introduction

Xysj2012: /* Indica Group */

2013-07-10T02:32:51Z

‎Indica Group

Xysj2012 at 02:31, 10 July 2013

2013-07-10T02:31:34Z

Xysj2012: /* Brief Introduction */

2013-07-10T02:31:08Z

‎Brief Introduction

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Xysj2012: Created page with "==Brief Introduction== * Basic helix–loop–helix (bHLH) transcription factors (TFs) constitute one of the largest families of transcription factors in three eukaryotic king..."

2013-07-10T02:30:38Z

Created page with "==Brief Introduction== * Basic helix–loop–helix (bHLH) transcription factors (TFs) constitute one of the largest families of transcription factors in three eukaryotic king..."

New page

==Brief Introduction==
* Basic helix–loop–helix (bHLH) transcription factors (TFs) constitute one of the largest families of transcription factors in three eukaryotic kingdoms<ref name="ref1" /><ref name="ref2" /><ref name="ref3" />.
[[File:bHLH_BGIOSGA030958.png|center|thumb|1000px|'''Figure 1.''' ''Protein Structure of '''BGIOSGA030958''''']]
* The bHLH domain contains approximately 60 amino acids, with two functionally distinctive regions: the basic region and the HLH region. The basic region is located at the N terminus of the bHLH domain consisted of 15 amino acids and functions as a DNA-binding motif. The HLH region contains two amphipathic a helices with a linking loop of variable lengths; the amphipathic a helices of two bHLH proteins can interact, allowing the formation of homodimers or heterodimers. Outside of the conserved bHLH domain, these proteins exhibit considerable sequence divergence<ref name="ref1" /><ref name="ref2" /><ref name="ref3" /><ref name="ref4" />.
* bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling，wound and drought stress responses， symbiotic ammonium transport， shoot branching，the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.

@@ Line 4: / Line 4: @@
 * The bHLH domain contains approximately 60 amino acids, with two functionally distinctive regions: the basic region and the HLH region. The basic region is located at the N terminus of the bHLH domain consisted of 15 amino acids and functions as a DNA-binding motif. The HLH region contains two amphipathic a helices with a linking loop of variable lengths; the amphipathic a helices of two bHLH proteins can interact, allowing the formation of homodimers or heterodimers. Outside of the conserved bHLH domain, these proteins exhibit considerable sequence divergence<ref name="ref1" /><ref name="ref2" /><ref name="ref3" /><ref name="ref4" />.
 * bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling, wound and drought stress responses, symbiotic ammonium transport, shoot branching, the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.
-*'''Pfam: [http://pfam.janelia.org/family/PF00010 PF00010]''' <font color=green>'''||'''</font>      '''InterPro: [http://www.ebi.ac.uk/interpro/entry/IPR001092 IPR001092]''' <font color=green>'''||'''</font>
+*'''Pfam: [http://pfam.janelia.org/family/PF00010 PF00010]''' <font color=green>'''||'''</font>      '''InterPro: [http://www.ebi.ac.uk/interpro/entry/IPR011598 IPR011598]''' <font color=green>'''||'''</font>
 ==''Japonica'' Group==

@@ Line 4: / Line 4: @@
 * The bHLH domain contains approximately 60 amino acids, with two functionally distinctive regions: the basic region and the HLH region. The basic region is located at the N terminus of the bHLH domain consisted of 15 amino acids and functions as a DNA-binding motif. The HLH region contains two amphipathic a helices with a linking loop of variable lengths; the amphipathic a helices of two bHLH proteins can interact, allowing the formation of homodimers or heterodimers. Outside of the conserved bHLH domain, these proteins exhibit considerable sequence divergence<ref name="ref1" /><ref name="ref2" /><ref name="ref3" /><ref name="ref4" />.
 * bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling, wound and drought stress responses, symbiotic ammonium transport, shoot branching, the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.
-*'''Pfam: [http://pfam.janelia.org/family/PF00010 PF06507]'''
+*'''Pfam: [http://pfam.janelia.org/family/PF00010 PF00010]''' <font color=green>'''||'''</font>      '''InterPro: [http://www.ebi.ac.uk/interpro/entry/IPR001092 IPR001092]''' <font color=green>'''||'''</font>
 ==''Japonica'' Group==

@@ Line 3: / Line 3: @@
 [[File:bHLH_BGIOSGA030958.png|center|thumb|1000px|'''Figure 1.''' ''Protein Structure of '''BGIOSGA030958''''']]
 * The bHLH domain contains approximately 60 amino acids, with two functionally distinctive regions: the basic region and the HLH region. The basic region is located at the N terminus of the bHLH domain consisted of 15 amino acids and functions as a DNA-binding motif. The HLH region contains two amphipathic a helices with a linking loop of variable lengths; the amphipathic a helices of two bHLH proteins can interact, allowing the formation of homodimers or heterodimers. Outside of the conserved bHLH domain, these proteins exhibit considerable sequence divergence<ref name="ref1" /><ref name="ref2" /><ref name="ref3" /><ref name="ref4" />.
-* bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling, wound and drought stress responses, symbiotic ammonium transport, shoot branching，the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.
+* bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling, wound and drought stress responses, symbiotic ammonium transport, shoot branching, the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.
 *'''Pfam: [http://pfam.janelia.org/family/PF00010 PF06507]'''

@@ Line 3: / Line 3: @@
 [[File:bHLH_BGIOSGA030958.png|center|thumb|1000px|'''Figure 1.''' ''Protein Structure of '''BGIOSGA030958''''']]
 * The bHLH domain contains approximately 60 amino acids, with two functionally distinctive regions: the basic region and the HLH region. The basic region is located at the N terminus of the bHLH domain consisted of 15 amino acids and functions as a DNA-binding motif. The HLH region contains two amphipathic a helices with a linking loop of variable lengths; the amphipathic a helices of two bHLH proteins can interact, allowing the formation of homodimers or heterodimers. Outside of the conserved bHLH domain, these proteins exhibit considerable sequence divergence<ref name="ref1" /><ref name="ref2" /><ref name="ref3" /><ref name="ref4" />.
-* bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling，wound and drought stress responses， symbiotic ammonium transport， shoot branching，the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.
+* bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling, wound and drought stress responses, symbiotic ammonium transport, shoot branching，the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.
 ==''Japonica'' Group==
 {| style="background:#A1A3A6; width:85%;" border="0"

@@ Line 370: / Line 370: @@
 '''[[BGIOSGA013493]]'''
 ||
-'''[[BGIOSGA040642]]'''
+'''[[BGIOSGA000262]]'''
 ||
 '''[[BGIOSGA006236]]'''
@@ Line 478: / Line 478: @@
 '''[[BGIOSGA027780]]'''
 ||
-'''[[BGIOSGA000262]]'''
 ||

@@ Line 1: / Line 1: @@
 ==Brief Introduction==
 * Basic helix–loop–helix (bHLH) transcription factors (TFs) constitute one of the largest families of transcription factors in three eukaryotic kingdoms<ref name="ref1" /><ref name="ref2" /><ref name="ref3" />.
-[[File:bHLH_BGIOSGA030958.png|center|thumb|1000px|'''Figure 1.''' ''Protein Structure of '''BGIOSGA030958''''']]
+[[File:bHLH_BGIOSGA030958.png|center|thumb|1000px|'''Figure 1.''' ''Gene Structure of '''BGIOSGA030958''''']]
 * The bHLH domain contains approximately 60 amino acids, with two functionally distinctive regions: the basic region and the HLH region. The basic region is located at the N terminus of the bHLH domain consisted of 15 amino acids and functions as a DNA-binding motif. The HLH region contains two amphipathic a helices with a linking loop of variable lengths; the amphipathic a helices of two bHLH proteins can interact, allowing the formation of homodimers or heterodimers. Outside of the conserved bHLH domain, these proteins exhibit considerable sequence divergence<ref name="ref1" /><ref name="ref2" /><ref name="ref3" /><ref name="ref4" />.
 * bHLHs represent key regulatory components in transcriptional networks controlling a number of biological processes. They have been reported to function in light signaling, hormone signaling, wound and drought stress responses, symbiotic ammonium transport, shoot branching, the development of fruit, flower, root, microspore, trichome and stomata<ref name="ref2" /><ref name="ref4" />.

← Older revision		Revision as of 02:31, 10 July 2013
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		+
		+	==References==
		+	<references>
		+	* <ref name="ref1">
		+	Heim M A, Jakoby M, Werber M, et al. The basic helix–loop–helix transcription factor family in plants: a genome-wide study of protein structure and functional diversity[J]. Molecular biology and evolution, 2003, 20(5): 735-747.</ref>
		+	* <ref name="ref2">
		+	Carretero-Paulet L, Galstyan A, Roig-Villanova I, et al. Genome-wide classification and evolutionary analysis of the bHLH family of transcription factors in Arabidopsis, poplar, rice, moss, and algae[J]. Plant physiology, 2010, 153(3): 1398-1412.
		+	</ref>
		+	* <ref name="ref3">
		+	Li X, Duan X, Jiang H, et al. Genome-wide analysis of basic/helix-loop-helix transcription factor family in rice and Arabidopsis[J]. Plant physiology, 2006, 141(4): 1167-1184.
		+	</ref>
		+	* <ref name="ref4">
		+	Toledo-Ortiz G, Huq E, Quail P H. The Arabidopsis basic/helix-loop-helix transcription factor family[J]. The Plant Cell Online, 2003, 15(8): 1749-1770.
		+	</ref>
		+	</references>