{"product_id":"mechanisms-in-transcriptional-regulation-9781405103701","title":"Mechanisms in Transcriptional Regulation","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003eMechanisms in Transcriptional Regulation  provides a concise discussion of the fundamental concepts in transcription and its regulation.\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003eList of boxes. \u003cp\u003ePreface.\u003c\/p\u003e \u003cp\u003eAcknowledgments.\u003c\/p\u003e \u003cp\u003e1 The vocabulary of transcription.\u003c\/p\u003e \u003cp\u003e1.1 Introduction 1.\u003c\/p\u003e \u003cp\u003e1.2 The vocabulary of transcription.\u003c\/p\u003e \u003cp\u003e1.2.1 RNA biogenesis.\u003c\/p\u003e \u003cp\u003e1.2.2 The transcriptional machinery.\u003c\/p\u003e \u003cp\u003e1.2.3 Cis-elements.\u003c\/p\u003e \u003cp\u003e1.3 Evolutionarily conserved mechanisms of transcription.\u003c\/p\u003e \u003cp\u003e1.3.1 Conservation across the three domains of life.\u003c\/p\u003e \u003cp\u003e1.3.2 Model eukaryotic organisms (and a plug for genetics).\u003c\/p\u003e \u003cp\u003e1.4 What’s coming up.\u003c\/p\u003e \u003cp\u003eProblems.\u003c\/p\u003e \u003cp\u003eFurther reading.\u003c\/p\u003e \u003cp\u003e2 RNA polymerases and the transcription cycle.\u003c\/p\u003e \u003cp\u003e2.1 Introduction.\u003c\/p\u003e \u003cp\u003e2.2 Core RNA polymerases.\u003c\/p\u003e \u003cp\u003e2.2.1 Bacterial core polymerases.\u003c\/p\u003e \u003cp\u003e2.2.2 Eukaryotic and archaeal core polymerases.\u003c\/p\u003e \u003cp\u003e2.3 Transcriptional elongation.\u003c\/p\u003e \u003cp\u003e2.3.1 Phosphoester linkage formation.\u003c\/p\u003e \u003cp\u003e2.3.2 Features of the ternary elongation complex.\u003c\/p\u003e \u003cp\u003e2.3.3 RNA polymerase as a motor.\u003c\/p\u003e \u003cp\u003e2.3.4 Elongation factors and backtracking.\u003c\/p\u003e \u003cp\u003e2.4 Transcriptional initiation.\u003c\/p\u003e \u003cp\u003e2.4.1 Distinct mechanisms for promoter recognition in bacteria and eukaryotes.\u003c\/p\u003e \u003cp\u003e2.4.2 Bacterial σ factors and promoter specificity.\u003c\/p\u003e \u003cp\u003e2.5 Transcriptional termination.\u003c\/p\u003e \u003cp\u003e2.5.1 Why terminate?.\u003c\/p\u003e \u003cp\u003e2.5.2 Termination in bacteria.\u003c\/p\u003e \u003cp\u003e2.5.3 Termination in eukaryotes.\u003c\/p\u003e \u003cp\u003e2.6 Summary.\u003c\/p\u003e \u003cp\u003eProblems.\u003c\/p\u003e \u003cp\u003eFurther reading.\u003c\/p\u003e \u003cp\u003e3 The eukaryotic basal machinery.\u003c\/p\u003e \u003cp\u003e3.1 Introduction.\u003c\/p\u003e \u003cp\u003e3.2 The class II core promoter.\u003c\/p\u003e \u003cp\u003e3.3 The catalog of factors.\u003c\/p\u003e \u003cp\u003e3.4 Pathway to the preinitiation complex.\u003c\/p\u003e \u003cp\u003e3.5 Promoter recognition and nucleation of the PIC by TFIID.\u003c\/p\u003e \u003cp\u003e3.5.1 TATA box recognition by TBP.\u003c\/p\u003e \u003cp\u003e3.5.2 TBP-associated factors and their function in TFIID.\u003c\/p\u003e \u003cp\u003e3.6 TFIIB: a functional analog of bacterial σ factors.\u003c\/p\u003e \u003cp\u003e3.6.1 TFIIB as a bridge between the promoter and polymerase.\u003c\/p\u003e \u003cp\u003e3.6.2 BRF, a TFIIB paralog in the class III machinery,and promoter melting.\u003c\/p\u003e \u003cp\u003e3.6.3 Functional similarity between TFIIB family proteins and σ.\u003c\/p\u003e \u003cp\u003e3.7 TFIIH in promoter opening and promoter clearance.\u003c\/p\u003e \u003cp\u003e3.7.1 A unique DNA helicase requirement for class II promoter opening.\u003c\/p\u003e \u003cp\u003e3.7.2 A connection between DNA repair and transcription.\u003c\/p\u003e \u003cp\u003e3.7.3 TFIIH and RNA polymerase II phosphorylation.\u003c\/p\u003e \u003cp\u003e3.8 Summary.\u003c\/p\u003e \u003cp\u003eProblems.\u003c\/p\u003e \u003cp\u003eFurther reading.\u003c\/p\u003e \u003cp\u003e4 Mechanisms of transcriptional activation.\u003c\/p\u003e \u003cp\u003e4.1 Introduction.\u003c\/p\u003e \u003cp\u003e4.2 Paradigms from E. coli.\u003c\/p\u003e \u003cp\u003e4.2.1 CRP: a sensor of the nutritional environment.\u003c\/p\u003e \u003cp\u003e4.2.2 λcI: regulator of the lysis\/lysogeny switch.\u003c\/p\u003e \u003cp\u003e4.2.3 Sequence-specific DNA recognition: the helix-turn-helix motif.\u003c\/p\u003e \u003cp\u003e4.2.4 Dimerization.\u003c\/p\u003e \u003cp\u003e4.2.5 Multiple targets for activators in the transcriptional machinery.\u003c\/p\u003e \u003cp\u003e4.2.6 How do activator–RNA polymerase contacts activate promoters?.\u003c\/p\u003e \u003cp\u003e4.3 Eukaryotic activators and their targets.\u003c\/p\u003e \u003cp\u003e4.3.1 The modular nature of eukaryotic activators.\u003c\/p\u003e \u003cp\u003e4.3.2 The Mediator: a special activator target in the eukaryotic transcriptional machinery.\u003c\/p\u003e \u003cp\u003e4.3.3 Release of Pol II from a paused state as a mechanism of activation.\u003c\/p\u003e \u003cp\u003e4.4 Summary.\u003c\/p\u003e \u003cp\u003eProblems.\u003c\/p\u003e \u003cp\u003eFurther reading.\u003c\/p\u003e \u003cp\u003e5 Transcriptional control through the modification of chromatin structure.\u003c\/p\u003e \u003cp\u003e5.1 Introduction.\u003c\/p\u003e \u003cp\u003e5.2 Chromatin structure.\u003c\/p\u003e \u003cp\u003e5.2.1 The nucleosome.\u003c\/p\u003e \u003cp\u003e5.2.2 Higher order chromatin structure.\u003c\/p\u003e \u003cp\u003e5.2.3 Euchromatin and heterochromatin.\u003c\/p\u003e \u003cp\u003e5.3 Histone modification.\u003c\/p\u003e \u003cp\u003e5.3.1 Lysine acetylation: diverse roles in gene activation.\u003c\/p\u003e \u003cp\u003e5.3.2 Lysine methylation: a chemically stable histone mark.\u003c\/p\u003e \u003cp\u003e5.3.3 Cross talk between histone marks.\u003c\/p\u003e \u003cp\u003e5.4 ATP-dependent chromatin remodeling enzymes.\u003c\/p\u003e \u003cp\u003e5.4.1 A diverse family of chromatin remodeling complexes.\u003c\/p\u003e \u003cp\u003e5.4.2 ATP-fueled motors for increasing DNA accessibility.\u003c\/p\u003e \u003cp\u003e5.4.3 Targeting of chromatin remodeling complexes.\u003c\/p\u003e \u003cp\u003e5.5 Protein motifs that recognize modified histones.\u003c\/p\u003e \u003cp\u003e5.5.1 Chromodomains.\u003c\/p\u003e \u003cp\u003e5.5.2 Bromodomains.\u003c\/p\u003e \u003cp\u003e5.6 Coordination of activator–coactivator interactions.\u003c\/p\u003e \u003cp\u003e5.7 Summary.\u003c\/p\u003e \u003cp\u003eProblems.\u003c\/p\u003e \u003cp\u003eFurther reading.\u003c\/p\u003e \u003cp\u003e6 Epigenetic control of transcription.\u003c\/p\u003e \u003cp\u003e6.1 Introduction.\u003c\/p\u003e \u003cp\u003e6.1.1 Common themes in epigenetics: a central role for histone methylation.\u003c\/p\u003e \u003cp\u003e6.2 Heterochromatic silencing.\u003c\/p\u003e \u003cp\u003e6.2.1 Chromosomal inheritance of the silent state.\u003c\/p\u003e \u003cp\u003e6.2.2 Histone methylation and maintenance of the silent state.\u003c\/p\u003e \u003cp\u003e6.2.3 Initiation of heterochromatic silencing.\u003c\/p\u003e \u003cp\u003e6.2.4 Evolutionary conservation of mechanisms for heterochromatic silencing.\u003c\/p\u003e \u003cp\u003e6.2.5 DNA methylation and heterochromatin.\u003c\/p\u003e \u003cp\u003e6.2.6 A distinct mechanism for heterochromatic silencing in budding yeast.\u003c\/p\u003e \u003cp\u003e6.3 Epigenetic control by Polycomb and Trithorax group proteins.\u003c\/p\u003e \u003cp\u003e6.3.1 Combinatorial control of segment identity.\u003c\/p\u003e \u003cp\u003e6.3.2 Establishment and maintenance phases of homeotic gene expression.\u003c\/p\u003e \u003cp\u003e6.3.3 Parallels between heterochromatic and PcG silencing.\u003c\/p\u003e \u003cp\u003e6.3.4 Maintenance of the active state by TrxG.\u003c\/p\u003e \u003cp\u003e6.3.5 A model for the epigenetic regulation of homeoticgene activity.\u003c\/p\u003e \u003cp\u003e6.4 X chromosome inactivation: parallels to heterochromatic and Polycomb group silencing.\u003c\/p\u003e \u003cp\u003e6.4.1 Random inactivation of the X chromosome.\u003c\/p\u003e \u003cp\u003e6.4.2 Cis-acting RNA in X inactivation.\u003c\/p\u003e \u003cp\u003e6.4.3 Histone modifications characteristic of both heterochromatic and PcG silencing on Xi.\u003c\/p\u003e \u003cp\u003e6.5 Summary.\u003c\/p\u003e \u003cp\u003eProblems.\u003c\/p\u003e \u003cp\u003eFurther reading.\u003c\/p\u003e \u003cp\u003e7 Combinatorial control in development and signal transduction.\u003c\/p\u003e \u003cp\u003e7.1 Introduction.\u003c\/p\u003e \u003cp\u003e7.2 Synergy and antagonism.\u003c\/p\u003e \u003cp\u003e7.2.1 Integration of regulatory inputs by cis-regulatory modules.\u003c\/p\u003e \u003cp\u003e7.2.2 The “AND” and “NOT” operators.\u003c\/p\u003e \u003cp\u003e7.3 Synergy and the enhanceosome.\u003c\/p\u003e \u003cp\u003e7.3.1 Enhanceosome assembly and architectural factors.\u003c\/p\u003e \u003cp\u003e7.3.2 Cooperative recruitment of coactivators by enhanceosomes.\u003c\/p\u003e \u003cp\u003e7.3.3 Sequential coactivator recruitment.\u003c\/p\u003e \u003cp\u003e7.4 Antagonism and stripe formation.\u003c\/p\u003e \u003cp\u003e7.4.1 Developmental regulatory networks.\u003c\/p\u003e \u003cp\u003e7.4.2 Short-range repression and stripe formation.\u003c\/p\u003e \u003cp\u003e7.5 Antagonism and the signal-mediated switch.\u003c\/p\u003e \u003cp\u003e7.5.1 Nuclear receptors: antagonism between coregulators.\u003c\/p\u003e \u003cp\u003e7.5.2 Receptor tyrosine kinase pathways: competition for a common DNA element.\u003c\/p\u003e \u003cp\u003e7.6 Summary.\u003c\/p\u003e \u003cp\u003eProblems.\u003c\/p\u003e \u003cp\u003eFurther reading.\u003c\/p\u003e \u003cp\u003eAnswers to problems.\u003c\/p\u003e \u003cp\u003eGlossary.\u003c\/p\u003e \u003cp\u003eIndex.\u003c\/p\u003e \u003cp\u003eColor plate section\u003c\/p\u003e","brand":"John Wiley and Sons Ltd","offers":[{"title":"Default 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