- Email: [email protected]
Nomenclature of eukaryotic DNA polymerases
XI
16. Hermenn, R., Huf, J., Bonhoeffar, F. (1972). Nature New Biol., 240, p. 235. 17. Konrad, E. B., Lehman, I. R. (1975). Proc. Nat. Aced. Sci. USA, 72, p. 2150. 18. Gottesman, MM., Hicks, M. L., Gellert, M. (1973). J. Mo/. Biol., 77, p. 531. 19. Konrad, E. B., Lehman, I. R. (1974). Proc. Net. Aced. Sol. USA, 71, p. 2048. 20. Olivera, B. M., Bonhoeffer, F. (1974). Nwfure, ~50, p. 513. 21. Weatergaard, O., Brutlag, D., Kornberg, A. (i972), J. Biol. Chem., 248, p. 1361. 22. Sugino, A., HIrose, S., Okazski, R. (1972). Proc, Net, Aced. Sci. USA, 69, p. 1863. 23. Kurosawa, Y., Ogawa, T., Hlrose, S., Okazakl, T., Okazaki, R. (1975). J. Mol. Biol., 96, p. 653. 24. Lark, K. G. (1972). Nature New Biol., 240, p. 237. 25. Louarn, J. M. (1974). Mo/ec. Gen, Genet.,
133, p. 193.
26. Bouche, J. P., Zachel, K., Kornberg, A. (1975). J. Biol. Chem., 250, p. 5995. 27. Nath, K., Hurwitz, J. (1974) J. Biol. Chem., 2~1, p. 3580.
28. Sig=l. N., Delius, H., Kornberg, T., Gefter, 29. 30. 31. 32. 33. 34. 35.
M. L., Alberta, B. (1972) Proc. Nat. Acad. Scl. USA, 69, p. 35-37. Wang, J. C. (1971) J. Mol. Biol., 55, p. 523. Livingston, O. M., Richardson, C. C. (1975). J, Biol. Chem., 250, p. 470. Hirota, Y., Ryter, A., Jacob, F. (1968). Cold Spring Harbor Syrup. Quant. Biol,, 33, p, 677. Wlcknar, S., Wright, M., Hurwitz, J. (1974). Proc. Nat. Acad. Sci. USA, 71, p. 783. Wickner, S., Berhower, I., Wright, M., Hurwltz, J. (1973). Proc. Net. Aced. Sci. USA, 70, p. 2389. Wecheler, J. A. (1975). J. Bact., 121, p. 594. FIlep, C. C., Allen, J. S., Gustafson, R. A.,
Allen, R. G., Walker, J. R. (1974). J. Bect., 119, p. 443. Jean-Michel LOUARN.
Pacific Grove, California from May 1115, 1975. This meeting (1) was attended by 4 8 scientists who discussed recent data concerning various DNA polymerases found in a number of eukaryotic species. Because of the proliferation of systems for naming the DNA polymerases, the conference attendees decided to establish a uniform system of nomenclature, It was decided to restrict the fist to those enzyme classes for which there is common agreement that they represent distinct entities, Four s u c h po/ymerase classes were identified, A fifth class of enzyme, the reverse transcriptases or RNA tumor virus-associated DNA polymerases, are distinctive enough not to need further identification (1). Other viral-induced DNA po/ymerases such as herpes (2) or vaccinia (3) induced DNA polymerases, can be referred to by the name of the causative virus, Consideration was given to devising a nomenclature connotating the size, cellular localization, or template preference of the various DNA polymerases, Such approaches were abandoned because of ambiguities and uncertainties inherent in them, Instead, it was decided that a system of Greek letters, assigned to the DNA po!ymerases according to the order of discovery, would be the most useful approach because it would differ from any of the systems previously used by ourselves and others. The nomenclature follows (2) :
proposed
is
as
Polymerase-¢, for the highmolecular-weight ( > 100,000) DNA polymerase, which was the first to be detected in mammalian cells (4), Even though this enzyme is often the major activity in cytoplasmic extracts of growing cells, its actual location, in v i v o , may be in the nucleus. It is particularly active in
1. D N A
Nomenclature of eukaryotic DNA polymerases A n o m e n c l a t u r e s y s t e m is proposed for the v a r i o u s D N A p o l y m e r a s e a c t i v i t i e s n o w k n o w n to e x i s t in e u k a r y o t i c cells.
An international conference on eukaryotic DNA polymerases, organized by David Korn of Stanford University, was held at the Asilomar Conference Center, 1975, 57, ~° 9.
(1) Supported by a grant (CA-17721) from the National Cancer Institute. Abstract booklets of this meeting are available from David Korn. (2) This nomenclature was first devised by David Baltimore, Fred J. Bollum, Robert C. Gallo, and Arthur Welssbach at a meeting held at the Massachusetts Institute of Technology on May 29, 1974. We acknowledge the assistance of Waldo E. Cohn, Director, Office of Biochemical Nomenclature, National Research Council.
XII
copying ¢ activated ~ double-stranded DNA (3), and has almost no ability to copy the oligo-homopelymer A . . d T ~ , The a-polymerase is strongly inhibited by reagents that block sulfhydryl groups, and isoelectric focusing experiments show it to be an acidic protein. It is free of nuclease activity. . D N A Polymerase-I~, f o r t h e l o w molecular-weight ( < 50,000) enzyme recovered almost entirely in nuclear extracts [6, Ii, 1, II, 9 ] . This enzyme is a basic protein and is resistant to reagents which block sulfhydryl groups. It copies activated DNA well and, to a somewhat lesser extent, the synthetic template A~.dTI~. It contains no detectable nuclease activity. . D N A Polymerase-~', for the most recently described DNA polymerase that copies A,.dT~.-, with high efficiency, but does not copy DNA well [10, I I ] . This enzyme has been called R-DNA polymerase to suggest its propensity for copying synthetic polyribonucleotides, but no evidence exists at present as to its ability to copy natural RNA. The y-polymerase is acidic, has a molecular weight > 100,000, and requires sulfhydryl-containing compounds for maximal activity. . Mitochondrial DNA Polymerase (DNA polymerase-mt) is an enzyme separable from the others [ I | , I | , 18] ; it is named for its subcellular localization, which is so characteristic of the enzyme. The Table shows h o w ~, ~, and T have been named in some previous publications by some workers. The nomenclature of DNA polymerases -a, -~, -T, and -mr is being and w i l l be utilized by us in the future (4). As new (3) Gapped, duplex DNA prepared by limited digestion of duplex DNA with DNaso I. (4) The descriptors ~, 13 and ~ should be attached to • polymerase t as above, but never to DNA, as in • the et-DNA polymerase ~, which gives an erroneous impression. Use of • t h e ad0olymerase ~, in proper context is acceptable. 1 9 7 5 , 57, n ° 9.
or different eukaryotic DNA polymerases are identified, the system could be expanded by the use of additional Greek or other symbols. It is our hope that others w i l l utilize this system in order to make the literature less ambiguous. It is also proposed that a standard unit of DNA polymerase activity be defined as that amount of enzyme catalyzing the incorporation of one nmol of total deoxynucleotide into a polymeric form in 60 minutes.
REFERENCES. 1. Temin, H. and D. Baltimore (1972). Adv. in Virus Res,, 17 (K. M. Smith and M. A. Lauffer, eds.), Academic Press, New York, pp. 129-186. 2. Keir, H. M., J. Hay, J. M. Morrison and J, Subak-Sharpe (1966). Nature, 210, 369-371. 3. Berns, K. I., C. Silverman and A. Weissbach (1969). J. Virol., 4, 15-23. 4. Yonede, M. and F. J. Bollum (1965). J. Biol. Chem., 240, 3385-3391. 5. Weissbach, A., A. Schlabach, B. Fridlender and A. Bolden (1971). Nature New Biol., 231, 167-170. 6. Chang, L. M. S. and F. J. 8ollum (1971). J. Biol. Chem., 246, 5835-5837. 7. Baril, E. F., O. E. Brown, M. D. Jenkins and J. Laszlo (1971). Biochemistry, 16, 19811992. 8. Chang, L. M. S. (1973) J. Biol. Chem., 248, 3789-3805. 9. Wang, T. S. F., W. D. Sedwick and D. Korn (1974). J. Biol. Chem., ?49, 841-950. 10. Fridlender, B., M. Fry, A. Bolden and A. Woissbach (1972). Proc. Nat. Acad. Sci. USA, 69, 452-455. 11. Lewis, B., J. Abrell, R. Smith and R. Gallo (1974). Science, 183, 867-869. 12. Meyer, R. and M. Simpson (1968). Proc. Nat. Acad. Sci. USA, 61, 130-137. 13. Kalf, G. F. and J. J. Ch'lh (1968}. J, BioL Chem., ?43, 4904-4916. 14. McCaffrey, R., D. F. Smoler and D. Baltimore (1974). Proc. Nat. Acad. Sci. USA, 70, 521-525. 15. Chang, L. M. S. and F. J. Bolium (1972). J. Biol. Chem., 247, 7948-7950. 16. Lewis, B. J., J. W. Abrell, R. G. Smith and R. C. Gallo (1974). Biochem. Biophys. Acta, 349, 148-160. 17. Sedwlck, W. D., T. S. F. Wang and D. Korn (1972). J. Biol. Chem., 247, 5026-6033. 18. Fry, M. and A. Welssbach (1973). Biochemistry, 12, 3602-3608.
XllI
SYSTEMS OF NAMING DNA POLYMERASES. Laboratory (Reference) Polymerams
DNA
Baltimore (14)
Bollum (15)
Gallo (16)
Korn (17}
G
C
6-8S (maxl) 3.4 S (mini)
I
cytoplasmic N2
N -f
A
II
III
Weissbach (18)
NI
Arthur Weissbach, Roche Institute of Molecular Biology, Nutley, New Jersey.
David Baltimore, Massachusetts Institute of Technology, Cambridge, Massachusetts.
Fred Bollum, University of Kentucky Medical Center. Lexington, Kentucky.
Robert Gallo, National Cancer Institute, Bethesda, Maryland.
David Korn, Stanford University, Palo Alto, California,
For the attendees at the Conference on Eukaryotic DNA Polymerases. Conf6rence
Euchem
& Galway, Irlande, du 6 au 8 juillet 1975
Le th~me de ce meeting est : Synthdse et modification des oligoet polysaccharides ~. Au programme figureront confdrences et groupes de discussions. Pour plus amples informations, s"adresser ~ : P. A. Finan, Conference Secretary, Dep. of Chemistry, University College, Galway, Irlande. 1975, 57, n ° 9.
XIV
S y m p o s i u m star le m R N A , e t sa relation s t r u c t u r e - f o n c t i o n & Gatlinburg (Tennessee) du 5 au 8 avril 1976 Ce symposium est organis~ par le Laboratoire National de Oak Ridge. Les thames choisis sont les suivants : Structure primaire de I'extr~mit~ 5" terminale ajoutde du poly A. R61e dans la synthase du mRNA et fonction ; S~quences des nucMotides des mRNAs purifi~s ; Problame de la maturitd du mRNA ; Chromation des matrices pour la transcription du mRNA ; ContrSle de la traduction. Pour tout renseignement compMmentaire, s'adresser ~ : Mrs J. Loop, Biology Division Oak Ridge National Laboratory, P.O. Box Y, Oak Ridge, Tennessee 37830.
X I P J o u r n 6 e s Biochimiques Latines & Bordeaux, France, du 31 mai au 3 juin 1976 Ces journ4es, organis~es par la SocMM de Chimie Biologique auront pour thames : m Associations lipides-protdines s~riques et membranaires ; m Interactions moMculaires entre acides nucMiques et prot~ines ; Membranes, structure et transport. Les communications auront lieu sous forme de posters. DMai d'envoi : 31 mars 1976. Pour tout autre renseignement, s"adresser au : Pr. J. E. Courtois, 4, avenue de rObservatoire, 75270 Paris Cedex 06. 1975, 57, n ° 9.
Cours sur les acides nucl4~ques et la syntlh~se p r c t 6 i q u e chez les v 6 g ~ a u x & Strasbourg, du 15 au 24 juillet 1976 Ce cours est parrain~ par le NATO, /'EMBO, ia FEBS et le CNRS. II consistera en conf6rences et en discussions sur les sujets suivants : DIVAs et RNAs des v~g~taux ; Synth&se prot~ique chez les v~g~taux et les systames ace//u/aires ; M~canismes de rdgulation contr61ant le DNA, le RNA et le m6tebolisme prot~ique chez les v6g6taux ; - - Virus des v~g6taux (structure, replication, traduction, aminoacylation de RNA s viraux ~ synthase de prot6ines virales).
-
-
-
-
Pour tout renseignement concernant /'organisation de ce cours, s'adresser soit au : Pr. L. Bogorad, The Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, Mass. 02138, U.S.A., soit au : Pr. J. H. Well, Institut de Biologie Mol~culaire et Cellulaire, 15, rue Descartes, 67000 Strasbourg, France.
Organisation et expression du g 6 n 6 m e e u c a r y o t e Ce symposium se tlendra & T6h6ran, Iran, du 2 au 6 mai 1976 Pour toutes informations, ~crire au : Dr. K. Javaherian, P.O. Box 14-1700, Teheran 14,/ran.
16. Hermenn, R., Huf, J., Bonhoeffar, F. (1972). Nature New Biol., 240, p. 235. 17. Konrad, E. B., Lehman, I. R. (1975). Proc. Nat. Aced. Sci. USA, 72, p. 2150. 18. Gottesman, MM., Hicks, M. L., Gellert, M. (1973). J. Mo/. Biol., 77, p. 531. 19. Konrad, E. B., Lehman, I. R. (1974). Proc. Net. Aced. Sol. USA, 71, p. 2048. 20. Olivera, B. M., Bonhoeffer, F. (1974). Nwfure, ~50, p. 513. 21. Weatergaard, O., Brutlag, D., Kornberg, A. (i972), J. Biol. Chem., 248, p. 1361. 22. Sugino, A., HIrose, S., Okazski, R. (1972). Proc, Net, Aced. Sci. USA, 69, p. 1863. 23. Kurosawa, Y., Ogawa, T., Hlrose, S., Okazakl, T., Okazaki, R. (1975). J. Mol. Biol., 96, p. 653. 24. Lark, K. G. (1972). Nature New Biol., 240, p. 237. 25. Louarn, J. M. (1974). Mo/ec. Gen, Genet.,
133, p. 193.
26. Bouche, J. P., Zachel, K., Kornberg, A. (1975). J. Biol. Chem., 250, p. 5995. 27. Nath, K., Hurwitz, J. (1974) J. Biol. Chem., 2~1, p. 3580.
28. Sig=l. N., Delius, H., Kornberg, T., Gefter, 29. 30. 31. 32. 33. 34. 35.
M. L., Alberta, B. (1972) Proc. Nat. Acad. Scl. USA, 69, p. 35-37. Wang, J. C. (1971) J. Mol. Biol., 55, p. 523. Livingston, O. M., Richardson, C. C. (1975). J, Biol. Chem., 250, p. 470. Hirota, Y., Ryter, A., Jacob, F. (1968). Cold Spring Harbor Syrup. Quant. Biol,, 33, p, 677. Wlcknar, S., Wright, M., Hurwitz, J. (1974). Proc. Nat. Acad. Sci. USA, 71, p. 783. Wickner, S., Berhower, I., Wright, M., Hurwltz, J. (1973). Proc. Net. Aced. Sci. USA, 70, p. 2389. Wecheler, J. A. (1975). J. Bact., 121, p. 594. FIlep, C. C., Allen, J. S., Gustafson, R. A.,
Allen, R. G., Walker, J. R. (1974). J. Bect., 119, p. 443. Jean-Michel LOUARN.
Pacific Grove, California from May 1115, 1975. This meeting (1) was attended by 4 8 scientists who discussed recent data concerning various DNA polymerases found in a number of eukaryotic species. Because of the proliferation of systems for naming the DNA polymerases, the conference attendees decided to establish a uniform system of nomenclature, It was decided to restrict the fist to those enzyme classes for which there is common agreement that they represent distinct entities, Four s u c h po/ymerase classes were identified, A fifth class of enzyme, the reverse transcriptases or RNA tumor virus-associated DNA polymerases, are distinctive enough not to need further identification (1). Other viral-induced DNA po/ymerases such as herpes (2) or vaccinia (3) induced DNA polymerases, can be referred to by the name of the causative virus, Consideration was given to devising a nomenclature connotating the size, cellular localization, or template preference of the various DNA polymerases, Such approaches were abandoned because of ambiguities and uncertainties inherent in them, Instead, it was decided that a system of Greek letters, assigned to the DNA po!ymerases according to the order of discovery, would be the most useful approach because it would differ from any of the systems previously used by ourselves and others. The nomenclature follows (2) :
proposed
is
as
Polymerase-¢, for the highmolecular-weight ( > 100,000) DNA polymerase, which was the first to be detected in mammalian cells (4), Even though this enzyme is often the major activity in cytoplasmic extracts of growing cells, its actual location, in v i v o , may be in the nucleus. It is particularly active in
1. D N A
Nomenclature of eukaryotic DNA polymerases A n o m e n c l a t u r e s y s t e m is proposed for the v a r i o u s D N A p o l y m e r a s e a c t i v i t i e s n o w k n o w n to e x i s t in e u k a r y o t i c cells.
An international conference on eukaryotic DNA polymerases, organized by David Korn of Stanford University, was held at the Asilomar Conference Center, 1975, 57, ~° 9.
(1) Supported by a grant (CA-17721) from the National Cancer Institute. Abstract booklets of this meeting are available from David Korn. (2) This nomenclature was first devised by David Baltimore, Fred J. Bollum, Robert C. Gallo, and Arthur Welssbach at a meeting held at the Massachusetts Institute of Technology on May 29, 1974. We acknowledge the assistance of Waldo E. Cohn, Director, Office of Biochemical Nomenclature, National Research Council.
XII
copying ¢ activated ~ double-stranded DNA (3), and has almost no ability to copy the oligo-homopelymer A . . d T ~ , The a-polymerase is strongly inhibited by reagents that block sulfhydryl groups, and isoelectric focusing experiments show it to be an acidic protein. It is free of nuclease activity. . D N A Polymerase-I~, f o r t h e l o w molecular-weight ( < 50,000) enzyme recovered almost entirely in nuclear extracts [6, Ii, 1, II, 9 ] . This enzyme is a basic protein and is resistant to reagents which block sulfhydryl groups. It copies activated DNA well and, to a somewhat lesser extent, the synthetic template A~.dTI~. It contains no detectable nuclease activity. . D N A Polymerase-~', for the most recently described DNA polymerase that copies A,.dT~.-, with high efficiency, but does not copy DNA well [10, I I ] . This enzyme has been called R-DNA polymerase to suggest its propensity for copying synthetic polyribonucleotides, but no evidence exists at present as to its ability to copy natural RNA. The y-polymerase is acidic, has a molecular weight > 100,000, and requires sulfhydryl-containing compounds for maximal activity. . Mitochondrial DNA Polymerase (DNA polymerase-mt) is an enzyme separable from the others [ I | , I | , 18] ; it is named for its subcellular localization, which is so characteristic of the enzyme. The Table shows h o w ~, ~, and T have been named in some previous publications by some workers. The nomenclature of DNA polymerases -a, -~, -T, and -mr is being and w i l l be utilized by us in the future (4). As new (3) Gapped, duplex DNA prepared by limited digestion of duplex DNA with DNaso I. (4) The descriptors ~, 13 and ~ should be attached to • polymerase t as above, but never to DNA, as in • the et-DNA polymerase ~, which gives an erroneous impression. Use of • t h e ad0olymerase ~, in proper context is acceptable. 1 9 7 5 , 57, n ° 9.
or different eukaryotic DNA polymerases are identified, the system could be expanded by the use of additional Greek or other symbols. It is our hope that others w i l l utilize this system in order to make the literature less ambiguous. It is also proposed that a standard unit of DNA polymerase activity be defined as that amount of enzyme catalyzing the incorporation of one nmol of total deoxynucleotide into a polymeric form in 60 minutes.
REFERENCES. 1. Temin, H. and D. Baltimore (1972). Adv. in Virus Res,, 17 (K. M. Smith and M. A. Lauffer, eds.), Academic Press, New York, pp. 129-186. 2. Keir, H. M., J. Hay, J. M. Morrison and J, Subak-Sharpe (1966). Nature, 210, 369-371. 3. Berns, K. I., C. Silverman and A. Weissbach (1969). J. Virol., 4, 15-23. 4. Yonede, M. and F. J. Bollum (1965). J. Biol. Chem., 240, 3385-3391. 5. Weissbach, A., A. Schlabach, B. Fridlender and A. Bolden (1971). Nature New Biol., 231, 167-170. 6. Chang, L. M. S. and F. J. 8ollum (1971). J. Biol. Chem., 246, 5835-5837. 7. Baril, E. F., O. E. Brown, M. D. Jenkins and J. Laszlo (1971). Biochemistry, 16, 19811992. 8. Chang, L. M. S. (1973) J. Biol. Chem., 248, 3789-3805. 9. Wang, T. S. F., W. D. Sedwick and D. Korn (1974). J. Biol. Chem., ?49, 841-950. 10. Fridlender, B., M. Fry, A. Bolden and A. Woissbach (1972). Proc. Nat. Acad. Sci. USA, 69, 452-455. 11. Lewis, B., J. Abrell, R. Smith and R. Gallo (1974). Science, 183, 867-869. 12. Meyer, R. and M. Simpson (1968). Proc. Nat. Acad. Sci. USA, 61, 130-137. 13. Kalf, G. F. and J. J. Ch'lh (1968}. J, BioL Chem., ?43, 4904-4916. 14. McCaffrey, R., D. F. Smoler and D. Baltimore (1974). Proc. Nat. Acad. Sci. USA, 70, 521-525. 15. Chang, L. M. S. and F. J. Bolium (1972). J. Biol. Chem., 247, 7948-7950. 16. Lewis, B. J., J. W. Abrell, R. G. Smith and R. C. Gallo (1974). Biochem. Biophys. Acta, 349, 148-160. 17. Sedwlck, W. D., T. S. F. Wang and D. Korn (1972). J. Biol. Chem., 247, 5026-6033. 18. Fry, M. and A. Welssbach (1973). Biochemistry, 12, 3602-3608.
XllI
SYSTEMS OF NAMING DNA POLYMERASES. Laboratory (Reference) Polymerams
DNA
Baltimore (14)
Bollum (15)
Gallo (16)
Korn (17}
G
C
6-8S (maxl) 3.4 S (mini)
I
cytoplasmic N2
N -f
A
II
III
Weissbach (18)
NI
Arthur Weissbach, Roche Institute of Molecular Biology, Nutley, New Jersey.
David Baltimore, Massachusetts Institute of Technology, Cambridge, Massachusetts.
Fred Bollum, University of Kentucky Medical Center. Lexington, Kentucky.
Robert Gallo, National Cancer Institute, Bethesda, Maryland.
David Korn, Stanford University, Palo Alto, California,
For the attendees at the Conference on Eukaryotic DNA Polymerases. Conf6rence
Euchem
& Galway, Irlande, du 6 au 8 juillet 1975
Le th~me de ce meeting est : Synthdse et modification des oligoet polysaccharides ~. Au programme figureront confdrences et groupes de discussions. Pour plus amples informations, s"adresser ~ : P. A. Finan, Conference Secretary, Dep. of Chemistry, University College, Galway, Irlande. 1975, 57, n ° 9.
XIV
S y m p o s i u m star le m R N A , e t sa relation s t r u c t u r e - f o n c t i o n & Gatlinburg (Tennessee) du 5 au 8 avril 1976 Ce symposium est organis~ par le Laboratoire National de Oak Ridge. Les thames choisis sont les suivants : Structure primaire de I'extr~mit~ 5" terminale ajoutde du poly A. R61e dans la synthase du mRNA et fonction ; S~quences des nucMotides des mRNAs purifi~s ; Problame de la maturitd du mRNA ; Chromation des matrices pour la transcription du mRNA ; ContrSle de la traduction. Pour tout renseignement compMmentaire, s'adresser ~ : Mrs J. Loop, Biology Division Oak Ridge National Laboratory, P.O. Box Y, Oak Ridge, Tennessee 37830.
X I P J o u r n 6 e s Biochimiques Latines & Bordeaux, France, du 31 mai au 3 juin 1976 Ces journ4es, organis~es par la SocMM de Chimie Biologique auront pour thames : m Associations lipides-protdines s~riques et membranaires ; m Interactions moMculaires entre acides nucMiques et prot~ines ; Membranes, structure et transport. Les communications auront lieu sous forme de posters. DMai d'envoi : 31 mars 1976. Pour tout autre renseignement, s"adresser au : Pr. J. E. Courtois, 4, avenue de rObservatoire, 75270 Paris Cedex 06. 1975, 57, n ° 9.
Cours sur les acides nucl4~ques et la syntlh~se p r c t 6 i q u e chez les v 6 g ~ a u x & Strasbourg, du 15 au 24 juillet 1976 Ce cours est parrain~ par le NATO, /'EMBO, ia FEBS et le CNRS. II consistera en conf6rences et en discussions sur les sujets suivants : DIVAs et RNAs des v~g~taux ; Synth&se prot~ique chez les v~g~taux et les systames ace//u/aires ; M~canismes de rdgulation contr61ant le DNA, le RNA et le m6tebolisme prot~ique chez les v6g6taux ; - - Virus des v~g6taux (structure, replication, traduction, aminoacylation de RNA s viraux ~ synthase de prot6ines virales).
-
-
-
-
Pour tout renseignement concernant /'organisation de ce cours, s'adresser soit au : Pr. L. Bogorad, The Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, Mass. 02138, U.S.A., soit au : Pr. J. H. Well, Institut de Biologie Mol~culaire et Cellulaire, 15, rue Descartes, 67000 Strasbourg, France.
Organisation et expression du g 6 n 6 m e e u c a r y o t e Ce symposium se tlendra & T6h6ran, Iran, du 2 au 6 mai 1976 Pour toutes informations, ~crire au : Dr. K. Javaherian, P.O. Box 14-1700, Teheran 14,/ran.