Abstract
Abstract The head-tail connector of phage λ, a protein knob inside the head shell to which the tail attaches, is composed primarily of head protein gpB § and its cleaved form gpB∗. All of the gpB and gpB∗ in the virion is located in the connector. gpFII, the protein that is thought to form the site on the head to which the tail binds, is also located in the connector. Head proteins gpE, gpD, X1 and X2 are not components of the connector. These assignments were made by disrupting virions with guanidine hydrochloride, in such a way that heads and tails separate with the connectors attached to the tails, and determining which head proteins co-purify with the tails. We find that lysates from a λE− infection contain a high proportion of tails with connectors attached. (Gene E codes for the major component of the head shell.) Connectors are also present on tails from a λE−C− infection, arguing that gpE, gpC, and their processed forms, X1 and X2, are all unnecessary for assembly of biologically competent connectors. The gpB in the connectors on E− and E−C− tails is in the uncleaved form. Connectors are not seen on tails from infections by λE−B−, λE−FII−, or λE− in a groE− host.
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