Green fluorescent protein /

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作者：edited by P. Michael Conn.

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ISBN：9780121822033

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Summary: Publisher Summary 1 One of the most important recent discoveries in science is the green fluorescent protein, isolated from a bioluminescent jellyfish. The gene that codes for this protein is active in any type of cell, from microbes to humans, producing a "day-glo" dye visible as a bright green light in the microscope. The power of the gene is that by using recombinant DNA technology. GFP can be spliced to any protein, essentially painting that protein green. When such a spliced protein is inside a cell. Further, time-lapse microscopy can be used to examine how that protein and the cellular components that it is part of move within the cell during the cell's life cycle. This Methods in Enzymologyvolume deals with the utility of green fluorescent protein (GFP). The OVID database (including MEDLINE, Current Contents, and other sources) lists nine references to GFP for the ten-year period 1985-1994. In contrast, in less than four years thereafter, over 500 references are listed, a testament to the rapid growth of interest in this probe. This volume documents many diverse uses for this interesting molecule in disciplines that broadly span biology. The methods presented include shortcuts and conveniences not included in previously published sources. The techniques are described in a context that allows comparisons to other related methodologies-such comparisons are valuable to readers who must adapt existing procedures to new systems. Also, so far as possible, methodologies have been presented in a manner that stresses their general applicability and potential limitations. The volume provides a substantial and current overview of the extant methodology in the field and a view of its rapid development. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymologyis one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences. Key Features * Monitoring of Physiological Processes * Localization of Molecules * Special Uses * Mutants * Variants of GFP Publisher Summary 2 One of the most important recent discoveries in science is the green fluorescent protein, isolated from a bioluminescent jellyfish. The gene that codes for this protein is active in any type of cell, from microbes to humans, producing a "day-glo" dye visible as a bright green light in the microscope. The power of the gene is that by using recombinant DNA technology. GFP can be spliced to any protein, essentially painting that protein green. When such a spliced protein is inside a cell. Further, time-lapse microscopy can be used to examine how that protein and the cellular components that it is part of move within the cell during the cell's life cycle. This Methods in Enzymologyvolume deals with the utility of green fluorescent protein (GFP). The OVID database (including MEDLINE, Current Contents, and other sources) lists nine references to GFP for the ten-year period 1985-1994. In contrast, in less than four years thereafter, over 500 references are listed, a testament to the rapid growth of interest in this probe. This volume documents many diverse uses for this interesting molecule in disciplines that broadly span biology. The methods presented include shortcuts and conveniences not included in previously published sources. The techniques are described in a context that allows comparisons to other related methodologies-such comparisons are valuable to readers who must adapt existing procedures to new systems. Also, so far as possible, methodologies have been presented in a manner that stresses their general applicability and potential limitations. The volume provides a substantial and current overview of the extant methodology in the field and a view of its rapid development. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymologyis one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences. Key Features * Monitoring of Physiological Processes * Localization of Molecules * Special Uses * Mutants * Variants of GFP

Table Of Contents:
CONTRIBUTORS TO VOLUME 302 ix(4)
PREFACE xiii(2)
VOLUMES IN SERIES xv
Section I. Monitoring of Physiological Processes 3(84)

1. Membrane Trafficking 3(8)

SABINE KUPZIG

SAN SAN LEE

GEORGE BANTING

2. Monitoring of Protein Secretion with Green Fluorescent Protein 11(9)

CHRISTOPH KAETHER

HANS-HERMANN GERDES

3. Green Fluorescent Protein to Visualize Cancer Progression and Metastasis 20(12)

ROBERT M. HOFFMAN

4. Comparison of Enhanced Green Fluorescent Protein and Its Destabilized Form as Transcription Reporters 32(6)

XIAONING ZHAO

TOMMY DUONG

CHIAO-CHIAN HUANG

STEVEN R. KAIN

XIANQIANG LI

5. Early Detection of Apoptosis with Annexin V-Enhanced Green Fluorescent Protein 38(5)

STEVEN R. KAIN

JING-TYAN MA

6. Green Fluorescent Protein in the Visualization of Particle Uptake and Fluid-Phase Endocytosis 43(8)

MARKUS MANIAK

7. Monitoring Intracellular Shuttling of Histidine-Rich pH-Sensor Proteins Tagged with Green Fluorescent Protein 51(7)

FRANK HANAKAM

GUNTHER GERISCH

8. Measuring Protein Degradation with Green Fluorescent Protein 58(15)

STEPHEN R. CRONIN

RANDOLPH Y. HAMPTON

9. Studying Nuclear Receptors with Green Fluorescent Protein Fusions 73(14)

GORDON L. HAGER
Section II. Localization of Molecules 87(102)

10. Localization of Calmodulin in Budding Yeast and Fission Yeast Using Green Fluorescent Protein 87(16)

MARK R. FLORY

TRISHA N. DAVIS

11. Analysis of Microtubule Organization and Dynamics in Living Cells Using Green Fluorescent Protein-Microtubule-Associated Protein 4 Chimeras 103(18)

KEITH R. OLSON

J. B. OLMSTED

12. Trafficking of the Androgen Receptor 121(15)

VIRGINIE GEORGET

BEATRICE TEROUANNE

JEAN-CLAUDE NICOLAS

CHARLES SULTAN

13. Use of Green Fluorescent Protein for Visualization of Cell-Specific Gene Expression and Subcellular Protein Localization in Bacillus subtilis 136(17)

CHRIS D. WEBB

ORNA RESNEKOV

14. Signaling, Desensitization, and Trafficking of G Protein-Coupled Receptors Revealed by Green Fluorescent Protein Conjugates 153(18)

LARRY S. BARAK

JIE ZHANG

STEPHEN S. G. FERGUSON

STEPHANE A. LAPORTE

MARC G. CARON

15. Use of Green Fluorescent Proteins Linked to Cytoskeletal Proteins to Analyze Myofibrillogenesis in Living Cells 171(18)

GUISSOU A. DABIRI

JOSEPH C. AYOOB

KENAN K. TURNACIOGLU

JEAN M. SANGER

JOSEPH W. SANGER
Section III. Special Uses 189(184)

16. Fluorescent Proteins in Single- and Multicolor Flow Cytometry 189(10)

LONNIE LYBARGER

ROBERT CHERVENAK

17. Flow Cytometric Analysis of Transcription: Use of Green Fluorescent Protein Variants to Control Transfection Efficiency 199(8)

LONNIE LYBARGER

ROBERT CHERVENAK

18. Use of Coexpressed Enhanced Green Fluorescent Protein as a Marker for Identifying Transfected Cells 207(6)

YU FANG

CHIAO-CHIAN HUANG

STEVEN R. KAIN

XIANQIANG LI

19. The Jellyfish Green Fluorescent Protein: A Tool for Studying Ion Channels and Second-Messenger Signaling in Neurons 213(12)

L. A. C. BLAIR

K. K. BENCE

J. MARSHALL

20. Expression of Green Fluorescent Protein and Inositol 1,4,5-Triphosphate Receptor in Xenopus laevis Oocytes 225(8)

ATSUSHI MIYAWAKI

JULIE M. MATHESON

LEE G. SAYERS

AKIRA MUTO

TAKAYUKI MICHIKAWA

TEIICHI FURUICHI

KATSUHIKO MIKOSHIBA

21. Expression of Green Fluorescent Protein in Transgenic Mice 233(17)

TATSUYUKI TAKADA

KENICHI YOSHIDA

KENJI NAKAMURA

KAZUKI NAKAO

GOZOH TSUJIMOTO

MOTOYA KATSUKI

SUMIO SUGANO

22. Green Fluorescent Protein as a Probe to Study Intracellular Solute Diffusion 250(14)

ALAN S. VERKMAN

23. Application of Green Fluorescent Protein-Protein A Fusion Protein to Western Blotting 264(8)

TAKASHI AOKI

KATHERINE S. KOCH

HYAM L. LEFFERT

HIROYUKI WATABE

24. Green Fluorescent Protein as a Reporter for Promoter Analysis of Testis-Specific Genes in Transgenic Mice 272(13)

P. PRABHAKARA REDDI

MARKO KALLIO

JOHN C. HERR

25. Green Fluorescent Protein in the Measurement of Bacteria-Host Interactions 285(11)

LUIZ E. BERMUDEZ

FELIX J. SANGARI

AMY PARKER

26. Flow Cytometric Analysis of Transgene Expression in Higher Plants: Green Fluorescent Protein 296(20)

DAVID W. GALBRAITH

LEONARD A. HERZENBERG

MICHAEL T. ANDERSON

27. Continual Green Fluorescent Protein Monitoring of Promoter Activity in Plants 316(13)

PETER E. URWIN

SIMON G. MOLLER

JENNIFER K. BLUMSOM

HOWARD J. ATKINSON

28. Retroviral Expression of Green Fluorescent Protein 329(12)

ILYA A. MAZO

JOHN P. LEVY

REBECCA R. MULDOON

CHARLES J. LINK, JR.

STEVEN R. KAIN

29. Confocal Imaging of Ca^(2+), pH, Electrical Potential, and Membrane Permeability in Single Living Cells 341(17)

JOHN J. LEMASTERS

DONNA R. TROLLINGER

TING QIAN

WAYNE E. CASCIO

HISAYUKI OHATA

30. In Vivo Retroviral Transduction and Expression of Green Fluorescent Protein 358(15)

JOHN P. LEVY

REBECCA R. MULDOON

ILYA A. MAZO

STEVEN R. KAIN

CHARLES J. LINK, JR.
Section IV. Mutants and Variants of Green Fluorescent Protein 373(78)

31. S147P Green Fluorescent Protein: A Less Thermosensitive Green Fluorescent Protein Variant 373(5)

YUKIO KIMATA

CHUN REN LIM

KENJI KOHNO

32. Spectral Variants of Green Fluorescent Protein 378(16)

GOTTFRIED J. PALM

ALEXANDER WLODAWER

33. Expression of Green Fluorescent Protein Using Baculovirus Vectors 394(14)

LINDA A. KING

CAROLE J. THOMAS

NICOLA WILKINSON

ROBERT D. POSSEE

34. Green Fluorescent Protein Forms for Energy Transfer 408(16)

ROGER HEIM

35. Use of Codon-Modified, Red-Shifted Variants of Green Fluorescent Protein Genes to Study Virus-Mediated Gene Transfer 424(14)

CHARLES J. LINK, JR.

SUMING WANG

REBECCA R. MULDOON

TATIANA SEREGINA

JOHN P. LEVY

36. Generation of a Destabilized Form of Enhanced Green Fluorescent Protein 438(6)

XIAONING ZHAO

XIN JIANG

CHIAO-CHIAN HUANG

STEVEN R. KAIN

XIANQIANG LI

37. Spectral Properties of Green Fluorescent Protein-S65A 444(7)

SATOSHI INOUYE

KAZUHIKO UMESONO

FREDERICK I. TSUJI
AUTHOR INDEX 451(26)
SUBJECT INDEX 477

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