Marketing Strategies Restaurant Leaders Use to Develop Their Customer Base

Surviving past the first year of operation is a growing concern for independent, full-service restaurants. Some restaurant leaders lack the marketing strategies necessary to develop a loyal customer base and survive beyond the first year of operation. The purpose of this multiple case study was to explore the marketing strategies that independent, family-oriented, full-service restaurant leaders located in the Pittsburgh, PA, metro area in business for at least 5 years have used to develop their customer base during the first year of operation. This study was guided by the 7Ps of marketing theory, which emphasizes how people, including customers and employees, influence the marketing process. Data were collected through in-depth semistructured interviews with 3 restaurant leaders and secondary documentation that included marketing and business strategies, customer base data, and profitability records during the first year of operation. Data were analyzed using a comparison analysis method to establish 3 emergent themes: immediate influence of word of mouth, power of consumer-driven marketing and social media, and the need for an integrated marketing mix. Findings indicate that these family-oriented, full-service restaurants were able to develop a customer base during their first year of business by integrating marketing strategies including word of mouth, social media, and limited print advertising. This study could assist these restaurant leaders in creating best practices for developing a customer base and surviving past the first year of operation. The implications for positive social change include the potential to empower restaurant leaders to engage in cause-related marketing, increase viability in local communities, and promote development of independent restaurants and small businesses

Cdc7p-Dbf4p Regulates Mitotic Exit by Inhibiting Polo Kinase

Cdc7p-Dbf4p is a conserved protein kinase required for the initiation of DNA replication. The Dbf4p regulatory subunit binds Cdc7p and is essential for Cdc7p kinase activation, however, the N-terminal third of Dbf4p is dispensable for its essential replication activities. Here, we define a short N-terminal Dbf4p region that targets Cdc7p-Dbf4p kinase to Cdc5p, the single Polo kinase in budding yeast that regulates mitotic progression and cytokinesis. Dbf4p mediates an interaction with the Polo substrate-binding domain to inhibit its essential role during mitosis. Although Dbf4p does not inhibit Polo kinase activity, it nonetheless inhibits Polo-mediated activation of the mitotic exit network (MEN), presumably by altering Polo substrate targeting. In addition, although dbf4 mutants defective for interaction with Polo transit S-phase normally, they aberrantly segregate chromosomes following nuclear misorientation. Therefore, Cdc7p-Dbf4p prevents inappropriate exit from mitosis by inhibiting Polo kinase and functions in the spindle position checkpoint

Budding Yeast Dbf4 Sequences Required for Cdc7 Kinase Activation and Identification of a Functional Relationship Between the Dbf4 and Rev1 BRCT Domains

Cdc7-Dbf4 is a two-subunit kinase required for initiating DNA replication. The Dbf4 regulatory subunit is required for Cdc7 kinase activity. Previous studies have shown that the C termini of Dbf4 orthologs encode a single (putative) C2H2 zinc (Zn) finger, referred to as “motif C.” By mutational analysis we show that the Zn finger is not required for the essential function of Dbf4. However, deletion and point mutants altering conserved Zn-finger residues exhibit a substantially slowed S-phase, DNA damage sensitivity, and a hypo-mutagenic phenotype following UV irradiation. Using two-hybrid and biochemical assays, we show that the Dbf4 Zn finger interacts with Cdc7 and stimulates its kinase activity. However, a separable Dbf4 region also mediates an interaction with Cdc7 such that only the loss of both Cdc7-interacting regions results in lethality. In contrast, an N-terminal BRCT-like domain is not required for induced mutagenesis nor does it interact with Cdc7. By making chimeric Dbf4 proteins that contain known BRCT domains in Saccharomyces cerevisiae, we show that the BRCT domain from Rev1, a translesion DNA polymerase, can uniquely substitute for the Dbf4 BRCT domain. Thus, we have mapped regions on budding yeast Dbf4 required for binding and activating Cdc7 kinase. Our data also suggest that the Dbf4 and Rev1 BRCT domains interact with a common protein or structure, although the precise function of both domains and their binding partners remains elusive