Skip Navigation

This Article
Right arrow Print PDF (357K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Funderud, S.
Right arrow Articles by Haugli, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Funderud, S.
Right arrow Articles by Haugli, F.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1977, Vol. 4, No. 2 405-413
© 1977


Articles

DNA replication in Physarum polycephalum: characterization of DNA replication products made in vivo in the presence of cycloheximide in strains sensitive and resistant to cycloheximide

Steinar Funderud and Finn Haugli

Institute of Medical Biology, University of Tromsø 9000 Tromsø, Norway

Received December 7, 1976. Synchronous plasmodia of cyclohfiximide-sensitive and cycloheximide-resistant strains of Physarum polycephalum were labelled with 3[H]-deoxyadenosine in pulse and pulse-chase experiments in presence and absence of cycloheximide. The replication products were studied with alkaline sucrose gradient sedimentation analysis. We show that the action of cycloheximide on DNA replication in Physarum is mediated through the ribosorae, since the ribosomally located resistance also -makes the plasmo-dial DNA replication refractile to the action of cycloheximide. Cycloheximide caused inhibition of three stages in DNA replication in the wild type: first, the formation of primary replication units ("Okazaki" size fragments), secondly, the ligation of primary units into secondary ("Replicon" size) units and thirdly, the ligation of secondary units into mature DNA.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Protein Sci.Home page
M. Horn, M. Baudys, Z. Voburka, I. Kluh, J. Vondrasek, and M. Mares
Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I)
Protein Sci., April 1, 2002; 11(4): 933 - 943.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
D. Greenbaum, A. Baruch, L. Hayrapetian, Z. Darula, A. Burlingame, K. F. Medzihradszky, and M. Bogyo
Chemical Approaches for Functionally Probing the Proteome
Mol. Cell. Proteomics, January 1, 2002; 1(1): 60 - 68.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. van der Spoel, E. Bonten, and A. d'Azzo
Processing of Lysosomal beta -Galactosidase. THE C-TERMINAL PRECURSOR FRAGMENT IS AN ESSENTIAL DOMAIN OF THE MATURE ENZYME
J. Biol. Chem., March 31, 2000; 275(14): 10035 - 10040.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
Y. V. Matsuka, S. Pillai, S. Gubba, J. M. Musser, and S. B. Olmsted
Fibrinogen Cleavage by the Streptococcus pyogenes Extracellular Cysteine Protease and Generation of Antibodies That Inhibit Enzyme Proteolytic Activity
Infect. Immun., September 1, 1999; 67(9): 4326 - 4333.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Okomoto, T. Minamikawa, G. Edward, V. Vakharia, and E. Herman
Posttranslational Removal of the Carboxyl-terminal KDEL of the Cysteine Protease SH-EP Occurs Prior to Maturation of the Enzyme
J. Biol. Chem., April 16, 1999; 274(16): 11390 - 11398.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Lalmanach, F. Lecaille, J. R. Chagas, E. Authie, J. Scharfstein, M. A. Juliano, and F. Gauthier
Inhibition of Trypanosomal Cysteine Proteinases by Their Propeptides
J. Biol. Chem., September 25, 1998; 273(39): 25112 - 25116.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Jerala, E. Zerovnik, J. Kidric, and V. Turk
pH-induced Conformational Transitions of the Propeptide of Human Cathepsin L. A ROLE FOR A MOLTEN GLOBULE STATE IN ZYMOGEN ACTIVATION
J. Biol. Chem., May 8, 1998; 273(19): 11498 - 11504.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. Illy, O. Quraishi, J. Wang, E. Purisima, T. Vernet, and JohnS. Mort
Role of the Occluding Loop in Cathepsin B Activity
J. Biol. Chem., January 10, 1997; 272(2): 1197 - 1202.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Brzin, B. Rogelj, T. Popovic, B. Strukelj, and A. Ritonja
Clitocypin, a New Type of Cysteine Proteinase Inhibitor from Fruit Bodies of Mushroom Clitocybe nebularis
J. Biol. Chem., June 30, 2000; 275(26): 20104 - 20109.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. Muller, A. Cameron, Y. Fortenberry, E. V. Apletalina, and I. Lindberg
Processing and Sorting of the Prohormone Convertase 2 Propeptide
J. Biol. Chem., December 8, 2000; 275(50): 39213 - 39222.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
O. Quraishi and A. C. Storer
Identification of Internal Autoproteolytic Cleavage Sites within the Prosegments of Recombinant Procathepsin B and Procathepsin S. CONTRIBUTION OF A PLAUSIBLE UNIMOLECULAR AUTOPROTEOLYTIC EVENT FOR THE PROCESSING OF ZYMOGENS BELONGING TO THE PAPAIN FAMILY
J. Biol. Chem., March 9, 2001; 276(11): 8118 - 8124.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
T. F. Kagawa, J. C. Cooney, H. M. Baker, S. McSweeney, M. Liu, S. Gubba, J. M. Musser, and E. N. Baker
From the Cover: Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine protease
PNAS, February 29, 2000; 97(5): 2235 - 2240.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.