Determination of gene product positions in bacteriophage T4 by specific antibody association

1970 ◽  
Vol 51 (2) ◽  
pp. 411-421 ◽  
Author(s):  
M. Yanagida ◽  
C. Ahmad-Zadeh
Keyword(s):  
Gene Product ◽  
Specific Antibody ◽  
Bacteriophage T4

scholarly journals P15 and P3, the Tail Completion Proteins of Bacteriophage T4, Both Form Hexameric Rings

2003 ◽  
Vol 185 (5) ◽  
pp. 1693-1700 ◽  
Author(s):  
Li Zhao ◽  
Shuji Kanamaru ◽  
Chatree'chalerm Chaidirek ◽  
Fumio Arisaka
Keyword(s):  
Electron Microscopy ◽  
Gene Product ◽  
Analytical Ultracentrifugation ◽  
Bacteriophage T4 ◽  
Sedimentation Equilibrium ◽  
Gene Products ◽  
Oligomeric State ◽  
Polypeptide Chains ◽  
Circular Dichroïsm

ABSTRACT Two proteins, gp15 and gp3 (gp for gene product), are required to complete the assembly of the T4 tail. gp15 forms the connector which enables the tail to bind to the head, whereas gp3 is involved in terminating the elongation of the tail tube. In this work, genes 15 and 3 were cloned and overexpressed, and the purified gene products were studied by analytical ultracentrifugation, electron microscopy, and circular dichroism. Determination of oligomerization state by sedimentation equilibrium revealed that both gp15 and gp3 are hexamers of the respective polypeptide chains. Electron microscopy of the negatively stained P15 and P3 (P denotes the oligomeric state of the gene product) revealed that both proteins form hexameric rings, the diameter of which is close to that of the tail tube. The differential roles between gp15 and gp3 upon completion of the tail are discussed.

Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers 1 1Edited by P. E. Wright

2000 ◽  
Vol 301 (4) ◽  
pp. 975-985 ◽  
Author(s):  
Petr G Leiman ◽  
Victor A Kostyuchenko ◽  
Mikhail M Shneider ◽  
Lidia P Kurochkina ◽  
Vadim V Mesyanzhinov ◽  
...  
Keyword(s):  
Gene Product ◽  
Bacteriophage T4 ◽  
Short Tail ◽  
Tail Fibers

Gene product dsbA of bacteriophage T4 binds to late promoters and enhances late transcription

1991 ◽  
Vol 225 (3) ◽  
pp. 427-434 ◽  
Author(s):  
Andreas Gansz ◽  
Ulrich Kruse ◽  
Wolfgang Rüger
Keyword(s):  
Gene Product ◽  
Bacteriophage T4 ◽  
Late Transcription

Role of the C-terminus in folding and oligomerization of bacteriophage T4 gene product 9

2008 ◽  
Vol 73 (9) ◽  
pp. 995-999
Author(s):  
L. P. Kurochkina ◽  
A. Yu. Vishnevskiy ◽  
V. V. Mesyanzhinov
Keyword(s):  
Gene Product ◽  
Bacteriophage T4 ◽  
C Terminus

Early role of the esc+ gene product in the determination of segments in Drosophila

Cell ◽  
1982 ◽  
Vol 31 (1) ◽  
pp. 285-292 ◽  
Author(s):  
Gary Struhl ◽  
Danny Brower
Keyword(s):  
Gene Product

scholarly journals Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices

1994 ◽  
Vol 124 (5) ◽  
pp. 855-863 ◽  
Author(s):  
H Zhang ◽  
SD Apfelroth ◽  
W Hu ◽  
EC Davis ◽  
C Sanguineti ◽  
...  
Keyword(s):  
Gene Product ◽  
Elastic Fiber ◽  
Extracellular Proteins ◽  
Connective Tissues ◽  
New Family ◽  
Fibrillin 1 ◽  
Partial Cdna ◽  
Point Determination ◽  
Human Chromosome 5

During the previous cloning of the fibrillin gene (FBN1), we isolated a partial cDNA coding for a fibrillin-like peptide and mapped the corresponding gene (FBN2) to human chromosome 5. (Lee, B., M. Godfrey, E. Vitale, H. Hori, M. G. Mattei, M. Sarfarazi, P. Tsipouras, F. Ramirez, and D. W. Hollister. 1991. Nature [Lond.]. 352:330-334). The study left, however, unresolved whether or not the FBN2 gene product is an extracellular component structurally related to fibrillin. Work presented in this report clarifies this important point. Determination of the entire primary structure of the FBN2 gene product demonstrated that this polypeptide is highly homologous to fibrillin. Immunoelectron microscopy localized both fibrillin proteins to elastin-associated extracellular microfibrils. Finally, immunohistochemistry revealed that the fibrillins co-distribute in elastic and non-elastic connective tissues of the developing embryo, with preferential accumulation of the FBN2 gene product in elastic fiber-rich matrices. These results support the original hypothesis that the fibrillins may have distinct but related functions in the formation and maintenance of extracellular microfibrils. Accordingly, we propose to classify the FBN1 and FBN2 gene products as a new family of extracellular proteins and to name its members fibrillin-1 and fibrillin-2, respectively.

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