Abstract
In previous studies it was shown that a DNA-free bacteriophage T7 procapsid (capsid I) draws DNA to its interior during assembly and as it begins this packaging capsid I changes in structure to capsid II. To probe the structures of capsids I and II, they have been digested with trypsin. The most abundant protein in the envelopes of capsids I and II, P10, was cleaved when capsid I was digested, but was not cleaved when capsid II was digested. Cleavage of capsid I-associated P10 formed a major P10 fragment 18% reduced in molecular weight, but did not detectably affect the size of capsid I (determined from sieving during agarose gel electrophoresis) or appearance of capsid I in the electron microscope. The magnitude of the (negative) average electrical surface charge density of capsid I was increased by digestion with trypsin (determined by agarose gel electrophoresis). At least one minor P10 fragment remained associated with capsid I after digestion.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 392-401 |
| Number of pages | 10 |
| Journal | Virology |
| Volume | 122 |
| Issue number | 2 |
| DOIs | |
| State | Published - Oct 30 1982 |
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ASJC Scopus subject areas
- Virology
- Infectious Diseases
Cite this
The structure of a bacteriophage T7 procapsid and its in Vivo conversion product probed by digestion with trypsin. / Serwer, Philip; Hayes, Shirley J.; Watson, Robert H.
In: Virology, Vol. 122, No. 2, 30.10.1982, p. 392-401.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The structure of a bacteriophage T7 procapsid and its in Vivo conversion product probed by digestion with trypsin
AU - Serwer, Philip
AU - Hayes, Shirley J.
AU - Watson, Robert H.
PY - 1982/10/30
Y1 - 1982/10/30
N2 - In previous studies it was shown that a DNA-free bacteriophage T7 procapsid (capsid I) draws DNA to its interior during assembly and as it begins this packaging capsid I changes in structure to capsid II. To probe the structures of capsids I and II, they have been digested with trypsin. The most abundant protein in the envelopes of capsids I and II, P10, was cleaved when capsid I was digested, but was not cleaved when capsid II was digested. Cleavage of capsid I-associated P10 formed a major P10 fragment 18% reduced in molecular weight, but did not detectably affect the size of capsid I (determined from sieving during agarose gel electrophoresis) or appearance of capsid I in the electron microscope. The magnitude of the (negative) average electrical surface charge density of capsid I was increased by digestion with trypsin (determined by agarose gel electrophoresis). At least one minor P10 fragment remained associated with capsid I after digestion.
AB - In previous studies it was shown that a DNA-free bacteriophage T7 procapsid (capsid I) draws DNA to its interior during assembly and as it begins this packaging capsid I changes in structure to capsid II. To probe the structures of capsids I and II, they have been digested with trypsin. The most abundant protein in the envelopes of capsids I and II, P10, was cleaved when capsid I was digested, but was not cleaved when capsid II was digested. Cleavage of capsid I-associated P10 formed a major P10 fragment 18% reduced in molecular weight, but did not detectably affect the size of capsid I (determined from sieving during agarose gel electrophoresis) or appearance of capsid I in the electron microscope. The magnitude of the (negative) average electrical surface charge density of capsid I was increased by digestion with trypsin (determined by agarose gel electrophoresis). At least one minor P10 fragment remained associated with capsid I after digestion.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020457430&partnerID=8YFLogxK
U2 - 10.1016/0042-6822(82)90238-0
DO - 10.1016/0042-6822(82)90238-0
M3 - Article
C2 - 7147708
AN - SCOPUS:0020457430
VL - 122
SP - 392
EP - 401
JO - Virology
JF - Virology
SN - 0042-6822
IS - 2
ER -