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Lipid Modifications of Proteins
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Main description:General Description of the Volume:This volume presents the best techniques and strategies for the study of lipid modified proteins, with particular emphasis on methods which evaluate the functional significance or biological impact of lipid modification. Included are the biological methods for the study of function (yeast genetics; cloning strategies; mutational analysis; expression systems), biochemical methods for the study and purification of enzymes or modified proteins (in vitro assays using peptide, native, or recombinant protein substrates; coupled in vitro cDNA transcr...
Main description:
General Description of the Volume:
This volume presents the best techniques and strategies for the study of lipid modified proteins, with particular emphasis on methods which evaluate the functional significance or biological impact of lipid modification. Included are the biological methods for the study of function (yeast genetics; cloning strategies; mutational analysis; expression systems), biochemical methods for the study and purification of enzymes or modified proteins (in vitro assays using peptide, native, or recombinant protein substrates; coupled in vitro cDNA transcription, translation/modification; bacolovirus expression; lipid analogs/inhibitors); physical methods for the identification of lipid groups (cleavage techniques; modification techniques; simple separations: TLC, GC, HPLC, ES/MS, tandem MS).
General Description of the Series:
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is 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.
Review quote:
Praise for the Volume
"...timely and useful... a very well-compiled volume... a substantive stimulus to those in the field, but it is also a very readable means for others to acquire a general introduction."
--James F. Riordan, Harvard Medical School, in ANALYTICAL BIOCHEMISTRY
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
--BIO/TECHNOLOGY
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
Table of contents:
Prenylation:
C.A. Omer, R.E. Diehl, and A.M. Kral, Bacterial Expression and Purification of Human Protein Prenyltransferases Using Epitope-Tagged, Translationally Coupled Systems.
J.F. Moomaw, F.L. Zhang, and P.J. Casey, Isolation of Protein Prenyltransferases from Bovine Brain and Baculovirus Expression System.
Y. Reiss, Substrate Interactions of Protein Prenyltransferases.
P.B. Cassidy, J.M. Dolence, and C.D. Poulter, Continuous Fluorescence Assay for Protein Prenyltransferases.
H. Mitsuzawa and F. Tamanoi, In Vivo Assays for Farnesyltransferase Inhibitors with Saccharomyces cerevisiae.
B.E. Caplin and M.S. Marshall, Mutagenesis and Biochemical Analysis of Recombinant Yeast Prenyltransferases.
D.A. Mitchell and R.J. Deschenes, Characterization of Protein Prenylation in Saccharomyces cerevisiae.
A.L. Wilson and W.A. Maltese, Coupled Translation/Prenylation of Rab Proteins in Vitro. Y. Fukada, Prenylation and Carboxylmethylation of G-Protein gamma Subunit.
A.D. Cox, Mutation and Analysis of Prenylation Signal Sequences.
Y. Takai, K. Kaibuchi, A. Kikuci, and T. Sasaki, Effects of Prenyl Modifications on Interactions of Small G Proteins with Regulators.
M.Dalton and M. Sinensky, Expression Systems for Nuclear Lamin Proteins: Farnesylation in Assembly of Nuclear Lamina.
J. Inglese, Prenylation-Dependent Targeting of G-Protein-Coupled Receptor Kinases.
J.A. Thissen, M.G. Barrett, and P.J. Casey, Prenylated Peptides in Identification of Specific Binding Proteins.
R.M. Epand, F. Naider, and J.M. Becker, Lipid-Mediated a-Factor Interactions with Artificial Membranes.
Prenylation-Dependent Processing:
L. Liu, G.-F. Jang, C.C.Farnsworth, K. Yokoyama, J.A. Glomset, and M.H. Gelb, Synthetic Prenylated Peptides: Studying Prenyl Protein-Specific Endoprotease and Other Aspects of Protein Prenylation.
B.A. Gilbert, Y.-T. Ma, and R.R. Rando, Inhibitors of Prenylated ProteinEndoprotease.
C. Volker, M.H. Pillinger, M.R. Philips, and J.B. Stock, Prenylcysteine Analogs to Study Function of Carboxylmethylation in Signal Transduction.
Y.-T. Ma, B.A. Gilbert, and R.R. Rando, Farnesylcysteine Analogs to Probe Role of Prenylated Protein Methyltransferase.
M.N. Ashby and J. Rine, Ras and a-Factor Converting Enzyme.
C.A. Hrycyna, S.J. Wait, P.S. Backlund, Jr., and S. Michaelis, Yeast STE14 Methyltransferase, Expressed as TrpE-STE14 Fusion Protein in Escherichia coli, for in Vitro Carboxylmethylation of Prenylated Polypeptides.
Palmitoylation:
B.M. Willumsen, Analysis of Ras Acylation Sites: Mutagenesis and Transfection.
S.I. Patterson and J.H.P. Skene, Inhibition of Dynamic Protein Palmitoylation in Intact Cells with Tunicamycin.
M. Bouvier, P. Chidiac, T.E. Hebert, T.P. Loisel, S. Moffett, and B. Mouillac, Dynamic Palmitoylation of G-Protein-Coupled Receptors in Eukaryotic Cells.
M.E. Linder, C. Kleuss, and S.M. Mumby, Palmitoylation of G-Protein ( Subunits.
A.I. Magee, J. Wootton, and J. de Bony, Detecting Radiolabeled Lipid-Modified Proteins in Polyacrylamide Gels.
L.A. Camp and S.L. Hofmann, Assay and Isolation of Palmitoyl-Protein Thioesterase from Bovine Brain Using Palmitoylated H-Ras as Substrate.
D.R. Pepperberg, D.F. Morrison, and P.J. OBrien, Depalmitoylation of Rhodopsin with Hydroxylamine.
O.A. Bizzozero, Chemical Analysis of Acylation Sites and Species.
Myristoylation:
S. Zozulya, D. Ladant, and L. Stryer, Expression and Characterization of Calcium-Myristoyl Switch Proteins.
P.A. Randazzo and R.A. Kahn, Myristoylation and ADP-Ribosylation Factor Function.
L.J. Knoll, D.R. Johnson, M.L. Bryant, and J.I. Gordon, Functional Significance of Myristoyl Moiety in N-Myristoyl Proteins.
P.A. Solski, L.A. Quilliam, S.G. Coats, C.J. Der, and J.E. Buss, Targeting Proteins to Membranes Using Signal Sequences for Lipid Modification.
L. Berthiaume, S.M. Peseckis, and M.D. Resh, Synthesis and Use of Iodo-Fatty Acid Analogs.
R.S. Bhatnagar and J.I. Gordon, Thermodynamic Studies of Myristoyl-CoA: Protein N-Myristoyltransferase Using Isothermal Titration Calorimetry.
T.A. Neubert and R.S. Johnson, High-Resolution Structural Determination of Protein-Linked Acyl Groups.
M. Chow and N. Moscufo, Myristoyl Modification of Viral Proteins: Assays to Assess Functional Roles. Glycosylphosphatidylinositol-Anchored Proteins:
J. Vidugiriene and A.K. Menon, Biosynthesis of Glycosylphosphatidylinositol Anchors.
K. Kodukula, S.E. Maxwell, and S. Udenfriend, Processing of Nascent Proteins to Glycosylphosphatidylinositol-Anchored Forms in Cell-Free Systems.
T. Kinoshita, T. Miyata, N. Inoue, and J. Takeda, Expression Cloning Strategies for Glycosylphosphatidylinositol-Anchor Biosynthesis Enzymes and Regulators.
S.D. Leidich, D.A. Drapp, and P. Orlean, Isolation and Characterization of Yeast Glycosylphosphatidylinositol Anchoring Mutants.
S. Udenfriend and K. Kodukula, Prediction of ( Site in Nascent Precursor of Glycosylphosphatidylinositol Protein.
S. Hirose, J.J. Knez, and M.E. Medof, Mammalian Glycosylphosphatidylinositol-Anchored Proteins and Intracellular Precursors.
P. Schneider and M.A.J. Ferguson, Microscale Analysis of Glycosylphosphatidylinositol Structures.
M.A. Deeg and M.A. Davitz, Glycosylphosphatidylinositol-Phospholipase D: A Tool for GlycosylphosphatidylinositolStructural Analysis.
K. Mensa-Wilmot, J.C. Morris, A. Al-Qahtani, and P.T. Englund, Purification and Use of Recombinant Glycosylphosphatidylinositol-Phospholipase C.
M.P. Lisanti, Z. Tang, P.E. Scherer, and M. Sargiacomo, Caveolae Purification and Glycosylphosphatidylinositol-Linked Protein Sorting in Polarized Epithelia.
K.G. Rothberg, Caveolar Targeting of Glycosylphosphatidylinositol-Anchored Proteins.
Other Modifications:
K.Sankaran, S.D. Gupta, and H.C. Wu, Modification of Bacterial Lipoproteins.
Author Index.
Subject Index.
General Description of the Volume:
This volume presents the best techniques and strategies for the study of lipid modified proteins, with particular emphasis on methods which evaluate the functional significance or biological impact of lipid modification. Included are the biological methods for the study of function (yeast genetics; cloning strategies; mutational analysis; expression systems), biochemical methods for the study and purification of enzymes or modified proteins (in vitro assays using peptide, native, or recombinant protein substrates; coupled in vitro cDNA transcription, translation/modification; bacolovirus expression; lipid analogs/inhibitors); physical methods for the identification of lipid groups (cleavage techniques; modification techniques; simple separations: TLC, GC, HPLC, ES/MS, tandem MS).
General Description of the Series:
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is 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.
Review quote:
Praise for the Volume
"...timely and useful... a very well-compiled volume... a substantive stimulus to those in the field, but it is also a very readable means for others to acquire a general introduction."
--James F. Riordan, Harvard Medical School, in ANALYTICAL BIOCHEMISTRY
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
--NEUROSCIENCE
"Incomparably useful."
--ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
--BIO/TECHNOLOGY
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."
--CHEMISTRY IN INDUSTRY
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
--AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
--ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
--JOURNAL OF CHROMATOGRAPHY
Table of contents:
Prenylation:
C.A. Omer, R.E. Diehl, and A.M. Kral, Bacterial Expression and Purification of Human Protein Prenyltransferases Using Epitope-Tagged, Translationally Coupled Systems.
J.F. Moomaw, F.L. Zhang, and P.J. Casey, Isolation of Protein Prenyltransferases from Bovine Brain and Baculovirus Expression System.
Y. Reiss, Substrate Interactions of Protein Prenyltransferases.
P.B. Cassidy, J.M. Dolence, and C.D. Poulter, Continuous Fluorescence Assay for Protein Prenyltransferases.
H. Mitsuzawa and F. Tamanoi, In Vivo Assays for Farnesyltransferase Inhibitors with Saccharomyces cerevisiae.
B.E. Caplin and M.S. Marshall, Mutagenesis and Biochemical Analysis of Recombinant Yeast Prenyltransferases.
D.A. Mitchell and R.J. Deschenes, Characterization of Protein Prenylation in Saccharomyces cerevisiae.
A.L. Wilson and W.A. Maltese, Coupled Translation/Prenylation of Rab Proteins in Vitro. Y. Fukada, Prenylation and Carboxylmethylation of G-Protein gamma Subunit.
A.D. Cox, Mutation and Analysis of Prenylation Signal Sequences.
Y. Takai, K. Kaibuchi, A. Kikuci, and T. Sasaki, Effects of Prenyl Modifications on Interactions of Small G Proteins with Regulators.
M.Dalton and M. Sinensky, Expression Systems for Nuclear Lamin Proteins: Farnesylation in Assembly of Nuclear Lamina.
J. Inglese, Prenylation-Dependent Targeting of G-Protein-Coupled Receptor Kinases.
J.A. Thissen, M.G. Barrett, and P.J. Casey, Prenylated Peptides in Identification of Specific Binding Proteins.
R.M. Epand, F. Naider, and J.M. Becker, Lipid-Mediated a-Factor Interactions with Artificial Membranes.
Prenylation-Dependent Processing:
L. Liu, G.-F. Jang, C.C.Farnsworth, K. Yokoyama, J.A. Glomset, and M.H. Gelb, Synthetic Prenylated Peptides: Studying Prenyl Protein-Specific Endoprotease and Other Aspects of Protein Prenylation.
B.A. Gilbert, Y.-T. Ma, and R.R. Rando, Inhibitors of Prenylated ProteinEndoprotease.
C. Volker, M.H. Pillinger, M.R. Philips, and J.B. Stock, Prenylcysteine Analogs to Study Function of Carboxylmethylation in Signal Transduction.
Y.-T. Ma, B.A. Gilbert, and R.R. Rando, Farnesylcysteine Analogs to Probe Role of Prenylated Protein Methyltransferase.
M.N. Ashby and J. Rine, Ras and a-Factor Converting Enzyme.
C.A. Hrycyna, S.J. Wait, P.S. Backlund, Jr., and S. Michaelis, Yeast STE14 Methyltransferase, Expressed as TrpE-STE14 Fusion Protein in Escherichia coli, for in Vitro Carboxylmethylation of Prenylated Polypeptides.
Palmitoylation:
B.M. Willumsen, Analysis of Ras Acylation Sites: Mutagenesis and Transfection.
S.I. Patterson and J.H.P. Skene, Inhibition of Dynamic Protein Palmitoylation in Intact Cells with Tunicamycin.
M. Bouvier, P. Chidiac, T.E. Hebert, T.P. Loisel, S. Moffett, and B. Mouillac, Dynamic Palmitoylation of G-Protein-Coupled Receptors in Eukaryotic Cells.
M.E. Linder, C. Kleuss, and S.M. Mumby, Palmitoylation of G-Protein ( Subunits.
A.I. Magee, J. Wootton, and J. de Bony, Detecting Radiolabeled Lipid-Modified Proteins in Polyacrylamide Gels.
L.A. Camp and S.L. Hofmann, Assay and Isolation of Palmitoyl-Protein Thioesterase from Bovine Brain Using Palmitoylated H-Ras as Substrate.
D.R. Pepperberg, D.F. Morrison, and P.J. OBrien, Depalmitoylation of Rhodopsin with Hydroxylamine.
O.A. Bizzozero, Chemical Analysis of Acylation Sites and Species.
Myristoylation:
S. Zozulya, D. Ladant, and L. Stryer, Expression and Characterization of Calcium-Myristoyl Switch Proteins.
P.A. Randazzo and R.A. Kahn, Myristoylation and ADP-Ribosylation Factor Function.
L.J. Knoll, D.R. Johnson, M.L. Bryant, and J.I. Gordon, Functional Significance of Myristoyl Moiety in N-Myristoyl Proteins.
P.A. Solski, L.A. Quilliam, S.G. Coats, C.J. Der, and J.E. Buss, Targeting Proteins to Membranes Using Signal Sequences for Lipid Modification.
L. Berthiaume, S.M. Peseckis, and M.D. Resh, Synthesis and Use of Iodo-Fatty Acid Analogs.
R.S. Bhatnagar and J.I. Gordon, Thermodynamic Studies of Myristoyl-CoA: Protein N-Myristoyltransferase Using Isothermal Titration Calorimetry.
T.A. Neubert and R.S. Johnson, High-Resolution Structural Determination of Protein-Linked Acyl Groups.
M. Chow and N. Moscufo, Myristoyl Modification of Viral Proteins: Assays to Assess Functional Roles. Glycosylphosphatidylinositol-Anchored Proteins:
J. Vidugiriene and A.K. Menon, Biosynthesis of Glycosylphosphatidylinositol Anchors.
K. Kodukula, S.E. Maxwell, and S. Udenfriend, Processing of Nascent Proteins to Glycosylphosphatidylinositol-Anchored Forms in Cell-Free Systems.
T. Kinoshita, T. Miyata, N. Inoue, and J. Takeda, Expression Cloning Strategies for Glycosylphosphatidylinositol-Anchor Biosynthesis Enzymes and Regulators.
S.D. Leidich, D.A. Drapp, and P. Orlean, Isolation and Characterization of Yeast Glycosylphosphatidylinositol Anchoring Mutants.
S. Udenfriend and K. Kodukula, Prediction of ( Site in Nascent Precursor of Glycosylphosphatidylinositol Protein.
S. Hirose, J.J. Knez, and M.E. Medof, Mammalian Glycosylphosphatidylinositol-Anchored Proteins and Intracellular Precursors.
P. Schneider and M.A.J. Ferguson, Microscale Analysis of Glycosylphosphatidylinositol Structures.
M.A. Deeg and M.A. Davitz, Glycosylphosphatidylinositol-Phospholipase D: A Tool for GlycosylphosphatidylinositolStructural Analysis.
K. Mensa-Wilmot, J.C. Morris, A. Al-Qahtani, and P.T. Englund, Purification and Use of Recombinant Glycosylphosphatidylinositol-Phospholipase C.
M.P. Lisanti, Z. Tang, P.E. Scherer, and M. Sargiacomo, Caveolae Purification and Glycosylphosphatidylinositol-Linked Protein Sorting in Polarized Epithelia.
K.G. Rothberg, Caveolar Targeting of Glycosylphosphatidylinositol-Anchored Proteins.
Other Modifications:
K.Sankaran, S.D. Gupta, and H.C. Wu, Modification of Bacterial Lipoproteins.
Author Index.
Subject Index.