Homomeric interactions between transmembrane proteins of Moloney murine leukemia virus.
We have studied homomeric interactions between transmembrane proteins (TM) of the Moloney murine leukemia virus envelope using the Saccharomyces cerevisiae two-hybrid system. TM interacts strongly with itself but not with various control proteins. Deletional and mutational analyses indicated that the putative leucine zipper motif in the extracellular domain of TM is essential and sufficient to mediate the binding. The first three repeats of the leucine zipper-like motif are the most important in mediating the interaction. The TM-TM interaction detected in this system may play a role in several stages of viral replication.
Li
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Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA.
McDermott
B
B
Yuan
B
B
Goff
S P
SP
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D016350:Leucine Zippers; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D008979:Moloney murine leukemia virus / Q000378:metabolism*; D011485:Protein Binding; D015682:Retroviridae Proteins, Oncogenic / Q000737:chemistry / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism*
D008565:Membrane Proteins; D015682:Retroviridae Proteins, Oncogenic; D014759:Viral Envelope Proteins; C078678:p15E protein, Murine leukemia virus