did-you-know? rent-now

Amazon no longer offers textbook rentals. We do!

did-you-know? rent-now

Amazon no longer offers textbook rentals. We do!

We're the #1 textbook rental company. Let us show you why.

9783527310197

Handbook of Photosensory Receptors

by ;
  • ISBN13:

    9783527310197

  • ISBN10:

    3527310193

  • Format: Hardcover
  • Copyright: 2005-04-15
  • Publisher: Vch Verlagsgesellschaft Mbh
  • Purchase Benefits
  • Free Shipping Icon Free Shipping On Orders Over $35!
    Your order must be $35 or more to qualify for free economy shipping. Bulk sales, PO's, Marketplace items, eBooks and apparel do not qualify for this offer.
  • eCampus.com Logo Get Rewarded for Ordering Your Textbooks! Enroll Now
  • Write a Review Icon Write a Review
List Price: $275.00

Summary

This first complete resource on photosensory receptors from bacteria, plants and animals compiles the data on all known classes of photoreceptors, creating a must-have reference for students and researchers for many years to come. Among the editors are the current and a former president of the American Society for Photobiology.

Author Biography

Winslow Briggs obtained his acadmic degrees from Harvard University almost fifty years ago. He spent most of his career at Stanford University, interrupted by a brief return to Harvard. He is currently professor emeritus of Stanford University and of the Carnegie Institution, where he is heading a research laboratory in the Department of Plant Biology. Professor Briggs has received numerous scientific awards including the Stephen Hales Prize of the American Society of Plant Physiologists and the Sterling Hendricks medal jointly bestowed by the USDA and the American Chemical Society. He is also a member of the National Academy of Sciences and a long-time editor of the Annual Review of Plant Physiology.

John Spudich received his PhD in biophysics from UC Berkeley working on chemotaxis, and conducted postdoctoral research on light-entrainment of circadian rhythms at Harvard and on photochemistry of retinal proteins at UCSF. In 1980, he joined the faculty of the Albert Einstein College of Medicine in New York. Since 1991 he is professor at the University of Texas Medical School at Houston, where he presently holds the Welch Distinguished Chair in Chemistry and is director of the Center for Membrane Biology. Professor Spudich recently received the Research Award of the American Society for Photobiology, as well as an NIH MERIT award. Together with Winslow Briggs, he has founded a new series of Gordon Conferences on Photosensory Receptors and Signal Transduction.

Table of Contents

Preface xvii
List of Authors xix
1 Microbial Rhodopsins: Phylogenetic and Functional Diversity
1(24)
John L. Spudich and Kwang-Hwan Jung
1.1 Introduction
1(1)
1.2 Archaeal Rhodopsins
2(5)
1.3 Clues to Newfound Microbial Rhodopsin Function from Primary Sequence Comparison to Archaeal Rhodopsins
7(3)
1.4 Bacterial Rhodopsins
10(6)
1.4.1 Green-absorbing Proteorhodopsin ("GPR") from Monterey Bay Surface Plankton
10(2)
1.4.2 Blue-absorbing Proteorhodopsin ("BPR") from Hawaiian Deep Sea Plankton
12(1)
1.4.3 Anabaena Sensory Rhodopsin
13(2)
1.4.4 Other Bacterial Rhodopsins
15(1)
1.5 Eukaryotic Microbial Rhodopsins
16(2)
1.5.1 Fungal Rhodopsins
16(1)
1.5.2 Algal Rhodopsins
17(1)
1.6 Spectral Tuning
18(1)
1.7 A Unified Mechanism for Molecular Function?
19(1)
1.8 Opsin-related Proteins without the Retinal-binding Site
20(1)
1.9 Perspective
20(1)
References
21(4)
2 Sensory Rhodopsin Signaling in Green Flagellate Algae
25(18)
Oleg A. Sineshchekov and John L. Spudich
2.1 Introduction
25(5)
2.1.1 Retinylidene Receptors
25(1)
2.1.2. Physiology of Algal Phototaxis and the Photophobic Response
26(1)
2.1.3 Photoelectrical Currents and their Relationship to Swimming Behavior
27(3)
2.2 The Photosensory Receptors: CSRA and CSRB
30(9)
2.2.1 Genomics, Sequence, and Predicted Structure
31(1)
2.2.2 Cellular Content and Roles in Phototaxis and Photophobic Behavior
32(4)
2.2.3 Molecular Mechanism of Action
36(3)
2.3 Other Algae
39(1)
2.4 Conclusion and Future Perspectives
40(1)
Acknowledgements
41(1)
References
41(2)
3 Visual Pigments as Photoreceptors
43(34)
Masato Kumauchi and Thomas Ebrey
3.1 Introduction
43(8)
3.1.1 General Considerations
43(6)
3.1.2 Photoreceptors and Pigments
49(1)
3.1.3 Non-photoreceptor or "Non-rod", "Non-cone" Retinal Pigments
50(1)
3.1.4 Retinal Photoisomerases
51(1)
3.2 The Unphotolyzed State of Vertebrate Visual Pigments
51(14)
3.2.1 Structure of Visual Pigments: the Chromophore
51(1)
3.2.2 Overall Topology of the Pigment
52(2)
3.2.3 Cytoplasmic Domain
54(1)
3.2.4 The Hydrophobic Core of Rhodopsin and the Retinal Binding Pocket
55(1)
3.2.5 The Extracellular Domain of Rhodopsin
56(1)
3.2.6 Structure of Other Visual Pigments
56(1)
3.2.7 Protonation State of Some of the Carboxylic Acids of Rhodopsin
57(1)
3.2.8 Internal Waters in Visual Pigments
57(1)
3.2.9 Is Rhodopsin a Dimer in vivo?
58(1)
3.2.10 Functional Properties of the Unphotolyzed State of a "Good" Visual Pigment
58(4)
3.2.11 Quantum Efficiency of Visual Pigment Photochemistry
62(1)
3.2.12 Dark Noise Originating from the Photoreceptor Pigment
63(2)
3.3 Activation of Vertebrate Visual Pigments
65(4)
3.3.1 Introduction
65(1)
3.3.2 The Primary Event, Photoisomerization
65(2)
3.3.3 The Meta I [-> Meta II Transition 66
3.3.4 Molecular Changes upon the Formation of Meta I and Meta II
67(1)
3.3.5 Internal Water Molecules
67(1)
3.3.6 Required Steps for Rhodopsin Activation
67(1)
3.3.7 The Transmembrane Signaling Pathway
68(1)
3.4 The Unphotolyzed State of Invertebrate Visual Pigments
69(2)
3.4.1 Introduction
69(1)
3.4.2 Wavelength Regulation of Invertebrate Pigments
70(1)
3.5 Mechanism of Activation of Invertebrate Visual Pigments
71(1)
3.5.1 The Initial Photochemical Events
71(1)
3.5.2 Formation of Acid Metarhodopsin
71(1)
3.5.3 Required Steps for Photolyzed Octopus Rhodopsin to Activate its G-protein
71(1)
3.5.4 Purification of the Active Form of an Invertebrate Visual Pigment
72(1)
Acknowledgements
72(1)
References
72(5)
4 Structural and Functional Aspects ofthe Mammalian Rod-Cell Photoreceptor Rhodopsin
77(16)
Najmoutin G. Abdulaev and Kevin D. Ridge
4.1 Introduction
77(2)
4.2 Rhodopsin and Mammalian Visual Phototransduction
79(1)
4.2.1 Signal Amplification by Light-activated Rhodopsin
79(1)
4.2.2 Inactivation of Light-activated Rhodopsin
79(1)
4.3 Properties of Rhodopsin
80(5)
4.3.1 Isolation of Rhodopsin
80(1)
4.3.2 Biochemical and Physicochemical Properties of Rhodopsin
81(1)
4.3.3 Post-translational Modifications in Rhodopsin
82(1)
4.3.4 Membrane Topology of Rhodopsin and Functional Domains
82(3)
4.4 Chromophore Binding Pocket and Photolysis of Rhodopsin
85(1)
4.5 Structure of Rhodopsin
86(2)
4.5.1 Crystal Structure of Rhodopsin
86(2)
4.5.2 Atomic Force Microscopy of Rhodopsin in the Disk Membrane
88(1)
4.6 Activation Mechanism of Rhodopsin
88(1)
4.7 Conclusions
89(1)
Acknowledgements
90(1)
References
90(3)
5 A Novel Light Sensing Pathway in the Eye: Conserved Features of Inner Retinal Photoreception in Rodents, Man and Teleost Fish
93(28)
Mark W. Hankins and Russell G. Foster
Summary
93(1)
5.1 Introduction
94(2)
5.1.1 A Novel Photoreceptor within the Eye
94(1)
5.1.2 Biological Clocks and their Regulation by Light
95(1)
5.2 Non-rod, Non-cone Photoreception in Rodents
96(8)
5.2.1 An Irradiance Detection Pathway in the Eye
96(1)
5.2.2 The Discovery of a Novel Ocular Photopigment in Mice (OP480)
97(2)
5.2.3 Melanopsin and Non-rod, Non-cone Photoreception
99(2)
5.2.4 A Functional Syncitium of Directly Light-sensitive Ganglion Cells
101(3)
5.3 Non-rod, Non-cone Photoreception in Humans
104(3)
5.3.1 Introduction
104(1)
5.3.2 Novel Photoreceptors Regulate Melatonin
105(1)
5.3.3 Novel Photoreceptors Regulate the Primary Visual Cone Pathway
105(2)
5.4 Non-rod, Non-cone Photoreception in Teleost Fish
107(5)
5.4.1 Background
107(1)
5.4.2 Vertebrate Ancient (VA) Opsin and Inner Retinal Photoreception in Teleost Fish
108(1)
5.4.3 A Novel Light Response from VA-opsin- and Melanopsin-expressing Horizontal Cells
108(1)
5.4.4 Action Spectra for the HC-RSD Light Response Identify a Novel Photopigment
109(2)
5.4.5 The Possible Function of HC-RSD Neurones
111(1)
5.5 Opsins can be Photosensors or Photoisomerases
112(1)
5.6 Placing Candidate Genes and Photopigments into Context
113(1)
5.7 Conclusions
114(1)
References
115(6)
6 The Phytochromes
121(30)
Shih-Long Tu and J. Clark Lagarias
6.1 Introduction
121(2)
6.1.1 Photomorphogenesis and Phytochromes
121(1)
6.1.2 The Central Dogma of Phytochrome Action
122(1)
6.2 Molecular Properties of Eukaryotic and Prokaryotic Phytochromes
123(4)
6.2.1 Molecular Properties of Plant Phytochromes
123(2)
6.2.2 Molecular Properties of Cyanobacterial Phytochromes
125(2)
6.3 Photochemical and Nonphotochemical Conversions of Phytochrome
127(6)
6.3.1 The Phytochrome Chromophore
127(2)
6.3.2 Phytochrome Photointerconversions
129(3)
6.3.3 Dark Reversion
132(1)
6.4 Phytochrome Biosynthesis and Turnover
133(9)
6.4.1 Phytobilin Biosynthesis in Plants and Cyanobacteria
133(5)
6.4.2 Apophytochrome Biosynthesis and Holophytochrome Assembly
138(3)
6.4.3 Phytochrome Turnover
141(1)
6.5 Molecular Mechanism of Phytochrome Signaling: Future Perspective
142(3)
6.5.1 Regulation of Protein-Protein Interactions by Phosphorylation
142(1)
6.5.2 Regulation of Tetrapyrrole Metabolism
143(2)
Acknowledgements
145(1)
References
145(6)
7 Phytochrome Signaling
151(20)
Enamul Huq and Peter H. Quail
7.1 Introduction
151(1)
7.2 Photosensory and Biological Functions of Individual Phytochromes
152(2)
7.3 phy Domains Involved in Signaling
154(10)
7.4 phy Signaling Components
155(1)
7.4.1 Second Messenger Hypothesis
155(1)
7.4.2 Genetically Identified Signaling Components
156(3)
7.4.3 phy-Interacting Factors
159(3)
7.4.4 Early phy-Responsive Genes
162(2)
7.5 Biochemical Mechanism of Signal Transfer
164(1)
7.6 phy Signaling and Circadian Rhythms
165(1)
7.7 Future Prospects
166(1)
Acknowledgements
167(1)
References
168(3)
8 Phytochromes in Microorganisms
171(26)
Richard D. Vierstra and Baruch Karniol
8.1 Introduction
171(1)
8.2 Higher Plant Phys
172(2)
8.3 The Discovery of Microbial Phys
174(2)
8.4 Phylogenetic Analysis of the Phy Superfamily
176(10)
8.4.1 Cyanobacterial Phy (Cph) Family
179(1)
8.4.2 Bacteriophytochrome (BphP) Family
179(5)
8.4.3 Fungal Phy (Fph) Family
184(1)
8.4.4 Phy-like Sequences
185(1)
8.5 Downstream Signal-Transduction Cascades
186(2)
8.6 Physiological Roles of Microbial Phys
188(3)
8.6.1 Regulation of Phototaxis
188(1)
8.6.2 Enhancement of Photosynthetic Potential
189(2)
8.6.3 Photocontrol of Pigmentation
191(1)
8.7 Evolution of the Phy Superfamily
191(1)
8.8 Perspectives
192(1)
Acknowledgements
193(1)
References
194(3)
9 Light-activated Intracellular Movement of Phytochrome
197(14)
Eberhard Schäfer and Ferenc Nagy
9.1 Introduction
197(1)
9.2 The Classical Methods
197(2)
9.2.1 Spectroscopic Methods
197(1)
9.2.2 Cell Biological Methods
198(1)
9.2.3 Immunocytochemical Methods
198(1)
9.3 Novel Methods
199(1)
9.4 Intracellular Localization of PHYB in Dark and Light
200(1)
9.5 Intracellular Localization of PHYA in Dark and Light
201(1)
9.6 Intracellular Localization of PHYC, PHYD and PHYE in Dark and Light
202(1)
9.7 Intracellular Localization of Intragenic Mutant Phytochromes
203(1)
9.7.1 Hyposensitive, Loss-of-function Mutants
203(1)
9.7.2 Hypersensitive Mutants
204(1)
9.8 Protein Composition of Nuclear Speckles Associated with phyB
204(3)
9.9 The Function of Phytochromes Localized in Nuclei and Cytosol
207(1)
9.10 Concluding Remarks
208(1)
References
209(2)
10 Plant Cryptochromes: Their Genes, Biochemistry, and Physiological Roles 211(36)
Alfred Batschauer
Summary
211(1)
10.1 Cryptochrome Genes and Evolution
212(2)
10.1.1 The Discovery of Cryptochromes
212(1)
10.1.2 Distribution of Cryptochromes and their Evolution
213(1)
10.2 Cryptochrome Domains, Cofactors and Similarities with Photolyase
214(5)
10.3 Biological Function of Plant Cryptochromes
219(13)
10.3.1 Control of Growth
220(3)
10.3.2 Role of Cryptochromes in Circadian Clock Entrainment and Photoperiodism
223(5)
10.3.3 Regulation of Gene Expression
228(4)
10.4 Localization of Cryptochromes
232(2)
10.5 Biochemical Properties of Cryptochromes
234(7)
10.5.1 Protein Stability
234(2)
10.5.2 Phosphorylation
236(3)
10.5.3 DNA Binding
239(1)
10.5.4 Electron Transfer
240(1)
10.6 Summary
241(1)
Acknowledgements
241(1)
References
242(5)
11 Plant Cryptochromes and Signaling 247(12)
Anthony R. Cashmore
11.1 Introduction
247(1)
11.2 Photolyases
247(1)
11.3 Cryptochrome Photochemistry
248(1)
11.4 Cryptochrome Action Spectra
249(1)
11.5 Cryptochromes and Blue Light-dependent Inhibition of Cell Expansion
250(1)
11.6 Signaling Mutants
251(1)
11.7 Signaling by Cryptochrome CNT and CCT Domains
251(1)
11.8 Arabidopsis Cryptochromes Exist as Dimers
252(1)
11.9 COP1, a Signaling Partner of Arabidopsis Cryptochromes
253(1)
11.10 Cryptochrome and Phosphorylation
253(1)
11.11 Cryptochrome and Gene Expression
254(1)
11.12 Concluding Thoughts
255(2)
References
257(2)
12 Animal Cryptochromes 259(18)
Russell N. Van Gelder and Aziz Sancar
12.1 Introduction
259(1)
12.2 Discovery of Animal Cryptochromes
260(1)
12.3 Structure-Function Considerations
260(3)
12.4 Drosophila melanogaster Cryptochrome
263(3)
12.5 Mammalian Cryptochromes, Circadian Rhythmicity, and Nonvisual Photoreception
266(7)
12.6 Cryptochromes of Other Animals
273(1)
12.7. Conclusions and Future Directions
274(1)
References
274(3)
13 Blue Light Sensing and Signaling by the Phototropins 277(28)
John M. Christie and Winslow R. Briggs
13.1 Introduction
277(1)
13.2 Phototropin Structure and Function
278(6)
13.2.1 Discovery of Phototropin
278(1)
13.2.2 Photl: a Blue Light-activated Receptor Kinase
279(1)
13.2.3 Phot2: a Second Phototropic Receptor
280(1)
13.2.4 Phototropins: Photoreceptors for Movement and More
281(2)
13.2.5 Overview of Phototropin Activation
283(1)
13.3 LOV Domain Structure and Function
284(6)
13.3.1 Light Sensing by the LOV Domains
284(2)
13.3.2 LOV is all Around
286(2)
13.3.3 Are Two LOVs Better than One?
288(2)
13.4 From Light Sensing to Receptor Activation
290(4)
13.4.1 LOV Connection
290(1)
13.4.2 Phototropin Autophosphorylation
291(1)
13.4.3 Phototropin Recovery
292(2)
13.5 Phototropin Signalling
294(6)
13.5.1 Beyond Photoreceptor Activation
294(1)
13.5.2 Phototropism
294(2)
13.5.3 Stomatal Opening
296(1)
13.5.4 Chloroplast Movement
297(2)
13.5.5 Rapid Inhibition of Hypocotyl Growth by Blue Light
299(1)
13.6 Future Prospects
300(1)
References
300(5)
14 LOV-domain Photochemistry 305(18)
Trevor E. Swartz and Roberto A. Bogomolni
14.1 Introduction
305(1)
14.2 The Chromoprotein Ground State Structure and Spectroscopy
306(6)
14.2.1 Structure of the Chromoprotein and its Chromophore Environment
306(1)
14.2.2 FMN Electrostatic Environment within the Protein
307(5)
14.3 Photochemistry
312(4)
14.3.1 Photocycle Kinetics and Structure of its Intermediates
312(4)
14.3.2 Photo-backreaction
316(1)
14.4 Reaction Mechanisms
316(4)
14.4.1 Adduct Formation
316(3)
14.4.2 Adduct Decay
319(1)
14.4 Future Perspectives
320(1)
References
321(2)
15 LOV-Domain Structure, Dynamics, and Diversity 323(14)
Sean Crosson
15.1 Overview
323(1)
15.2 LOV Domain Architecture and Chromophore Environment
324(2)
15.3 Photoexcited-State Structural Dynamics of LOV Domains
326(2)
15.4 Comparative Structural Analysis of LOV Domains
328(6)
15.5 LOV-Domain Diversity 330 Acknowledgements
334(1)
References
335(2)
16 The ZEITLUPE Family of Putative Photoreceptors 337(12)
Thomas F. Schultz
16.1 Introduction
337(1)
16.2 Circadian Clocks
337(3)
16.3 SCF Ubiquitin Ligases
340(1)
16.4 Photoperception
341(1)
16.5 The ZTL Gene Family
342(4)
16.5.1 ZTL
343(1)
16.5.2 FKF1
344(1)
16.5.3 LKP2
345(1)
16.6 Summary
346(1)
References
346(3)
17 Photoreceptor Gene Families in Lower Plants 349(22)
Noriyuki Suetsugu and Masamitsu Wada
17.1 Introduction
349(3)
17.2 Cryptochromes
352(5)
17.2.1 Adiantum capillus-veneris
352(2)
17.2.2 Physcomitrella patens
354(2)
17.2.3 Chlamydomonas reinhardtii
356(1)
17.3 Phototropins
357(6)
17.3.1 Adiantum capillus-veneris
357(1)
17.3.2 Physcomitrella patens
358(3)
17.3.3 Chlamydomonas reinhardtii
361(2)
17.4 Phytochromes in Lower Plants
363(3)
17.4.1 Conventional Phytochromes
363(1)
17.4.2 Phytochrome 3 in Polypodiaceous Ferns
364(2)
17.5 Concluding Remarks
366(1)
Acknowledgements
366(1)
References
367(4)
18 Neurospora Photoreceptors 371(20)
Jay C. Dunlap and Jennifer J. Loros
18.1 Introduction and Overview
371(1)
18.2 The Photobiology of Fungi in General and Neurospora in Particular
371(4)
18.2.1 Photoresponses are Widespread
371(1)
18.2.2 Photobiology of Neurospora
372(3)
18.3 Light Perception - the Nature of the Primary Blue Light Photoreceptor
375(2)
18.3.1 Flavins as Chromophores
375(1)
18.3.2 Genetic Dissection of the Light Response
375(1)
18.3.3 New Insights into Photoreceptors from Genomics
376(1)
18.4 How do the Known Photoreceptors Work?
377(7)
18.4.1 WC-1 and WC-2 contain PAS Domains and Act as a Complex
377(1)
18.4.2 WC-1 is the Blue Light Photoreceptor
378(4)
18.4.3 Post-activation Regulation of WC-1
382(1)
18.4.4 A Non-photobiological Role for WC-1 and the WCC
383(1)
18.5 VIVID, a Second Photoreceptor that Modulates Light Responses
384(3)
18.5.1 Types of Photoresponse Modulation
384(2)
18.5.2 Proof of VVD Photoreceptor Function
386(1)
18.6 Complexities in Light Regulatory Pathways
387(1)
18.7 Summary and Conclusion
387(1)
References
388(3)
19 Photoactive Yellow Protein, the Xanthopsin 391(26)
Michael A. van der Horst, Johnny Hendriks, Jocelyne Vreede, Sergei Yeremenko, Wim Crielaard and Klaas J. Hellingwerf
19.1 Introduction
391(3)
19.1.1 Discovery of the Photoactive Yellow Protein
391(1)
19.1.2 A Family of Photoactive Yellow Proteins: the Xanthopsins
392(1)
19.1.3 Differentiation of Function among the Xanthopsins
392(1)
19.1.4 PYP: The Prototype PAS Domain
393(1)
19.2 Structure
394(3)
19.2.1 Primary, Secondary, and Tertiary Structure
394(1)
19.2.2 Solution Structure vs. Crystal Structure
395(1)
19.2.3 The Xanthopsins Compared
396(1)
19.3 Photoactivity of the Xanthopsins
397(4)
19.3.1 The Basic Photocycle
397(2)
19.3.2 Photocycle Nomenclature
399(1)
19.3.3 Experimental Observation: Context Dependence
399(1)
19.3.4 Mutants and Hybrids
400(1)
19.3.5 Photo-activation in the Different Xanthopsins Compared
400(1)
19.4 The Photocycle of Photoactive Yellow Protein
401(7)
19.4.1 Initial Events
401(2)
19.4.2 Signaling State Formation and Ground State Recovery
403(1)
19.4.3 Structural Relaxation of pR
404(1)
19.4.4 Protonation Change upon pB' Formation
404(1)
19.4.5 Structural Change upon pB Formation
405(2)
19.4.6 Recovery of the Ground State
407(1)
19.5 Spectral Tuning of Photoactive Yellow Protein
408(3)
19.5.1 Ground State Tuning
409(1)
19.5.2 Spectral Tuning in Photocycle Intermediates
410(1)
19.6 Summary and Future Perspective
411(1)
References
412(5)
20 Hypericin-like Photoreceptors 417(16)
Pill-Soon Song
Abstract
417(1)
20.1 Introduction
417(3)
20.2 Ciliate Photoreceptors
420(5)
20.2.1 Action Spectra
420(1)
20.2.2 The Chromophores
421(2)
20.2.3 Proteins and Localization
423(2)
20.3 Photochemistry
425(2)
20.3.1 Photosensitization?
425(1)
20.3.2 Primary Photoprocesses
425(2)
20.4 Photosensory Signal Transduction
427(3)
20.4.1 Signal Generation
428(1)
20.4.2 Signal Amplification
429(1)
20.4.3 Signal Transduction
429(1)
20.5 Concluding Remarks
430(1)
Acknowledgements
430(1)
References
431(2)
21 The Antirepressor AppA uses the Novel Flavin-Binding BLUF Domain as a Blue-Light-Absorbing Photoreceptor to Control Photosystem Synthesis 433(14)
Shinji Masuda and Carl E. Bauer
21.1 Overview
433(1)
21.2 Oxygen and Light Intensity Control Synthesis of the Bacterial Photosystem
434(4)
21.2.1 PpsR is a DNA-binding Transcription Factor that Coordinates both Oxygen and Light Regulation
435(1)
21.2.2 Discovery of AppA, a Redox Responding, Blue Light Absorbing, Antirepressor of PpsR
435(3)
21.3 Mechanism of the BLUF Photocycle in AppA
438(3)
21.4 Other BLUF Containing Proteins
441(2)
21.5 Concluding Remarks
443(1)
Acknowledgement
444(1)
References
444(3)
22 Discovery and Characterization of Photoactivated Adenylyl Cyclase (PAC), a Novel Blue-Light Receptor Flavoprotein, from Euglena gracilis 447
Masakatsu Watanabe and Mineo Iseki
22.1 Introduction
447(1)
22.2 Action Spectroscopy
447(2)
22.3 PAC Discovery and its Identification as the Blue-light Receptor for Photoavoidance
449(7)
22.4 PAC Involvement in Phototaxis
456(1)
22.5 PAC Origin
457(1)
22.6 Future Prospects
457(2)
Acknowledgements
459(1)
References
460

Supplemental Materials

What is included with this book?

The New copy of this book will include any supplemental materials advertised. Please check the title of the book to determine if it should include any access cards, study guides, lab manuals, CDs, etc.

The Used, Rental and eBook copies of this book are not guaranteed to include any supplemental materials. Typically, only the book itself is included. This is true even if the title states it includes any access cards, study guides, lab manuals, CDs, etc.

Rewards Program